杰出校友(第二期) – Outstanding Alumni (Issue Two)

Issue Two (March 2002)

黄若青 Ruoqing Huang | 张鲁榕 Lurong Zhang | 雷振民 Zhenmin Lei | 阮克和 Kehe Ruan

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黄若青

黄若青 RUOQING HUANG, M.D., Ph.D.

“Thank you, Ruoqing and other founding leaders of AAFMUA”

2/23/2002

Dear Friends and Alumni,

The first term of leaders of AAFMUA had completed their tenure and relayed their responsibility to the second term of leaders in New York on Feb. 23, 2002. At this moment, I would like to share my feeling and comments with you on the founding leaders. To be honest, I just know some of them. So my comments cover only a few of them. If you have any comments, please send email to us, and we will be happy to post them in the Alumni Garden at AAFMUA website.

One night two years ago, I received a phone call at about 10pm from Dr. Ruoqing Huang. I was in California, and Ruoqing was in New York, so the time was 1am in New York. Ruoqing told me that he just got home and wanted to talk with me about a plan to establish Fujian Medical College Alumni Association in North America (AAFMUA). Ruoqing was then a resident of Surgical Pathology in Cornell University. Everybody knows how busy it is as a medical resident in USA. No wonder he had no time rather than midnight to make phone calls. I received many Ruoqing’s “midnight phone calls” in the past two years. To be honest, I myself did not have enough energy and enthusiasm to work for AAFMUA at midnight. I once asked Ruoqing what was his motivation to initiate the establishment of AAFMUA, since he was so busy already, and it was a pure volunteer work without personal benefit. His answer was simple and clear: “I just want to do something that I think is good for our Alumni and our alma mater, FMU.”

As the founding president, Ruoqing and other leaders such as Drs Ling Zheng, Ken Chen, Tongchuan Li, and Yishun Lin spent tremendous time and energy on setting up the Association and organizing all kinds of activities. They published the directory of FMU Alumni. The directory is so helpful for us to contact our old classmates and friends. Using the directory, my wife Yanfei got help from our alumni in different cities when she was traveling all over the country for her medical residency interviews. They established an exchange program between alumni in USA and those in FMU so that many of our alumni have the opportunity to have postdoctoral training in USA, and many of our alumni in USA became the guest professors of FMU and went to visit FMU and gave lectures there. I am sure this program will expedite the progress in medical service, research and teaching in FMU. They set up the AAFMUA website to promote the communication among alumni in USA and in FMU. They have done many other things that are benefiting us. I feel grateful to Ruoqing and other founding leaders for what they have done for our community. I believe many of our alumni have the same feeling.

Ruoqing told me that he would continue to do his best to help our alumni and our alma mater FMU. He said “it is just a sense of community.” I believe many of our alumni have the same feeling. We all want to help each other and make our community better. Many good communities constitute a strong country.

Wish our friends and alumni have a happy and successful 2002!

Sincerely,

Defu

Defu Zeng, MD
Senior Research Scientist
Division of Immunology & Rheumatology
Department of Medicine
Stanford University School of Medicine
Stanford, CA 94305
Tel: 650-723-5545 (Lab); 650-947-8772 (Home); Fax: 650-723-3347

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张鲁榕

“I consider medical research as life-long interest.”

张鲁榕 LURONG ZHANG, M.D., Ph.D.

Dr. Lurong Zhang is currently a Research Associate Professor in Department of Oncology, Lombardi Cancer Center, Georgetown University, Washington DC. Her current interests of research are in the following areas: 1) Role of angiogenesis factors (FGF, ECM1) on tumor progression; 2) Hyaluronan, hyaluronan synthase, hyaluronidase, CD44 and tumor progression; 3) Anti-tumor mechanisms of hyaluronan binding proteins, truncated HA binding proteins and HA binding motifs; 3) Identification of receptors and signal pathway for hyaluronan binding proteins and ECM1; 4). Explore new anti-tumor small molecule, which inhibits telomerase. If you want to know more details, please read her representative publications attached at the end.

Dr. Zhang obtained her MD from Fujian Medical University in 1982, and PhD from the Second Medical College, Shanghai in 1989. She did her postdoctoral training in Department of Pharmaceutical Sciences, College of Pharmacy, Idaho State University from 1990 to 1991, and in Department of Drug Discovery, Bristol-Myers Squibb Pharmaceutical Research Institute, Seattle from 1991 to 1992, and in Lombardi Cancer Center, School of Medicine, Georgetown University, Washington DC from 1992 to 1994. She was subsequently promoted to Research Assistant Professor in 1994 and Research Associate Professor in 1999 at School of Medicine, Georgetown University. Dr. Zhang currently has 6 grants from NIH and other foundations.

Dr. Zhang deeply cares about our alma mater FMU. She is one of the professors who are most actively having collaborations with colleagues at FMU. If you want to contact Dr. Zhang, her address is

WG06, Dept of Oncology
Georgetown University Medical Center
3970 Reservoir Road, NW
Washington DC, 20007
Tel: 202-687-6397
Fax: 202-687-7505

HOME ADDRESS:
8506 Bradmoor Drive
Bethesda, MD 20817

Eamil: zhangl@georgetown.edu

Representative Publications:

1. Zhang L; Kharbanda S; Chen D; Bullocks J; Miller DL; Ding IY; Hanfelt J; McLeskey SW; Kern FG: MCF-7 breast carcinoma cells overexpressing FGF-1 form vascularized, metastatic tumors in ovariectomized or tamoxifen-treated nude mice. Oncogene 1997; 15 (17): 2093-108

2. Zhang L; Kharbanda S; Hanfelt J; Kern FG: Both autocrine and paracrine effects of transfected acidic fibroblast growwth factor are involved in the estrogen-independent and antiestrogen-resistant growth of MCF-7 breast cancer cells. Cancer Res 1998; 8 (2): 352-61.

3. Lurong Zhang, Samir Kharbanda, Sandra W. Mcleskey and Francis G.Kern: Overexpression of fibroblast growth factor 1 in MCF-7 breast cancer cells facilitates tumor cell dissemination but does not support the development of macrometastases in the lung or lymph nodes. Cancer Res. 1999; 59: 5023-5029

4. Underhill,C.B. and Lurong Zhang: Analysis of hyaluronan using biotinylated hyaluronan-Binding proteins. Method in Mol. Biol. 2000; 137: 441-447

5. Zeqiu Han, Jian Ni, Patrick Smits, Charles B. Underhill, Bin Xie, Ningfei Liu, Przemko Tylzanowski, David Parmelee, Ping Feng, Ivan Ding, Feng Gao, Reiner Gentz, Danny Huylebroeck, Jozef Merregaert and Lurong Zhang : Extracellular matrix protein 1(ECM1): a novel angiogenic factor expressed in breast cancer cells. FASEB J: 2001; 988-994

6. Ningfei Liu, Charles B. Underhill, Randall Lapevich , Zeqiu Han, Feng Gao, Lurong Zhang and Shawn Green: Metastatin: A hyaluronan binding complex from cartilage that inhibits tumor growth. Cancer Res 2001; 61:1022-1028

7. Yixin Chen, XueMing Xu, Shuigen Hong, Jinguo Chen, Ningfei Liu, Charles B. Underhill, Karen Creswell and Lurong Zhang: RGD-Tachyplesin inhibits tumor growth. Cancer Res. 2001; 61: 2434-2438

8. Ningfei Liu, Feng Gao, Zeqiu Han, Charles B. Underhill and Lurong Zhang: Over-expression of Human Hyaluronan Synthase 3 in TSU Prostate Cancer Cells Promotes Tumor Growth . Cancer Res.2001, 61: 5207-5214
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雷振民

“I am hunting for the new roles of Gonadotropins.”

雷振民 ZHENMIN LEI, M.D., Ph.D.

Dr. Zhenmin Lei is currently an Associate Professor at Department of Obstetrics/Gynecology and Woman’s Health, School of Medicine, University of Louisville, Louisville, Kentucky. Dr. Lei has done excellent research in determining the biological and clinical importance of luteinizing hormone/human chorionic gonadotropin (LH/hCG) receptors in gonadal as well as non-gonadal tissues. More specifically, his research includes: (1) the pathophysiologic and molecular mechanism(s) underlying the regulation of gonadal and non-gonadal tissue functions by LH and hCG in both male and female; (2) use of LH receptor knockout mice to determine the importance of gonadal and nongonadal LH signaling; (3) Develop double LH receptor and follicle stimulating hormone (FSH) receptor knockout; (4) Develop conditional LH receptor knockout by Cre-LoxP system; (5) Direct roles of LH and/or hCG in breast, prostate and endometrial cancers and choriocarcinoma; (6) Potential clinical uses of hCG in improving pregnancy rates in assisted reproductive technologies, in the treatment of threatened and habitual abortions, preterm labor, breast cancer prevention/treatment, reproductive tract infections, HIV and spinal cord injuries. Additional laboratory interest includes the study of the mechanism(s) and physiologic impact of the age-related changes in gonadotropin deficient animals. If you want to know more about his research, please read his representative publications attached at the end.

Dr. Lei obtained his MD from Fujian Medical University in 1980, MS from Tianjin Medical College in 1984, and PhD from Department of Biochemistry and Molecular Biology, School of Medicine, University of Louisville in 1995. Dr. Lei went through his postdoctoral training in the Division of Reproductive Endocrinology, Department of Obstetrics & Gynecology, School of Medicine, University of Louisville from 1987 to 1990. He was recruited as an assistant professor in the same Department in 1995 and promoted to Associate Professor in 2001. Dr. Lei currently has two NIH grants. There are currently four postdoctoral fellows and PhD students in his lab. Dr. Lei is ad-hoc reviewer of Journals such as Endocrinology, Fertility and Sterility, Biology of Reproduction, Molecular and Cellular Endocrinology, and Journal of Clinical Endocrinology and Metabolism; he is also a reviewer for grant agencies such as Physiology & Pharmacology Panel, The Wellcome Trust Human Embryology and Development 1 Study Section, NIH.

Dr. Lei is a guest professor of FMU. He would like to have collaborations with alumni and colleagues in USA or at FMU. If you want to contact Dr. Lei for collaboration or postdoctoral position, his address is

Business Address: Dept. of OB/GYN, School of Medicine, University of Louisville, 438 MDR Building, Louisville, KY 40292
Business Phone: (502) 852-5509
Fax: (502) 852-0881
E-mail: zhenmin.lei@louisville.edu
Home Address: 3106 Stonebridge Road, Louisville, KY
Home Phone: (502) 426-5919

Representative Publications:

1. Rao CV, Lei ZM (2002) Consequences of targeted inactivation of LH receptors. Mol Cell Endocrinol (In Press).

2. Lei ZM and Rao ChV (2001) Neural actions of luteinizing hormone and human chorionic gonadotropin. Sem Reprod Med 19:103-109.

3. Eblen A, Bao S, Lei ZM, Nakajima ST, Rao ChV (2001) The presence of functional luteinizing hormone/human chorionic gonadotropin receptors in human sperm. J Clin Endocrinol Metab 86:2643-2648.

4. Lei ZM, Mishra S, Zou W, Xu B, Foltz M, Li X, Rao ChV (2001) Targeted disruption luteinizing hormone/human chorionic gonadotropin receptor gene. Mol Endocrinol 15:184-200.

5. Corley DR, Li X, Lei ZM, Rao ChV (2000) Potential regulation of gonadotropin-releasing hormone gene by steroidogenic factor-1-like protein. Mol Hum Reprod 6:671-676.

6. Akerman FM, Lei ZM, Rao ChV, Nakajima ST (2000) hCG receptor defect leading to a case of spontaneous ovarian hyperstimulation syndrome. Fert Steril 74:403-404.

7. Jauniaux E, Bao S, Eblen A, Li X, Lei ZM, Meuris S, Rao ChV (2000) hCG concentration and receptor gene expression in placental tissue from trisomy 18 and 21. Mol Hum Reprod 6:5-10.

8. Zhang W, Lei ZM, Rao ChV (1999) Immortalized hippocampal neurons contain functional luteinizing hormone/human chorionic gonadotropin receptors. Life Sci 65:2083-2098.

9. Kurtzman JT, Spinnato JA, Goldsmith LJ, Zimmerman MJ, Klem M, Lei ZM, Rao ChV (1999) Human chorionic gonadotropin exhibits potent inhibition of preterm delivery in a small animal model. Am J Obstet Gynecol 181:853-857.

10. Han S.W., Z.M. Lei and Rao ChV (1999) Treatment of human endometrial stromal cells with chorionic gonadotropin promotes their morphological and functional differentiation into decidua. Mol Cell Endrinol 147:7-16

11. Hu YL, Lei ZM, Rao ChV (1999) Determinants of transcription the chorionic gonadotropin/luteinizing hormone receptors gene in human breast cells. Breast J 5:186-193.

12. Lei ZM, Taylor DD, Gercel-Taylor C, Rao ChV (1999) Tumorigenic potential of human chorionic gonadotropin in choriocarcinoma JAR cells. Trophoblast Res 13:147-160.

13. Zhou XL, Lei ZM, Rao ChV (1999) Treatment of human endometrial gland epithelial cells with chorionic gonadotropin/luteinizing hormone increases the expression of cyclooxygenase-2 gene. J Clin Endocrinol Metab 84:3364-3377.

14. Hu YL, Lei ZM, Rao, ChV (1998) Analysis of the promoter of the luteinizing hormone/human chorionic gonadotropin receptor gene in neuroendocrine cells. Life Sci 63:2157-2165.

15. Tao YX, Heit M, Lei ZM, Rao ChV (1998) The urinary bladder of a woman is a novel site of luteinizing hormone-human chorionic gonadotropin receptor gene expression. Am J Obstet Gynecol 179:1026-1031.

16. Thompson DA, Othman MI, Lei ZM, Li X, Huang ZH, Eadie DM, Rao ChV (1998) Localization of the receptor for luteinizing hormone/chorionic gonadotropin in neural retina. Life Sci 63:1057-1064.

17. Bian L, Lei ZM, Rao ChV (1998) Mitogen activated protein kinase is involved in epidermal growth factor regulated protein phosphorylation in nuclear membranes isolated from JEG-3 human choriocarcinoma cells. Eur J Biochem 253:545-551.

18. Bird JS, Li X, Lei ZM, Sanfilippo J, Yussman MA, Rao ChV (1998) Luteinizing hormone and chorionic gonadotropin decrease type 2 5-alpha reductase and androgen receptor protein levels in women’s skin. J Clin Endocrinol Metab 83:1776-1782.

19. Tao YX, Lei ZM, Rao ChV (1998) Novel expression of luteinizing hormone/human chorionic gonadotropin receptor gene in rat seminal vesicles. J Andrology 19:343-347.

20. Al-Hader AA, Lei ZM, Rao ChV (1997) Fetal rat brains contain functional luteinizing hormone/human chorionic gonadotropin receptors. Early Pregnancy: Biol Med 3:323-329.

21. Al-Hader AA, Lei ZM, Rao ChV (1997) Novel expression of functional luteinizing hormone/human chorionic gonadotropin receptors in cultured glial cells from neonatal rat brains contain. Biol Reprod 56:501-507.

22. Lojun S, Bao S, Lei ZM, Rao ChV (1997) The presence of functional luteinizing hormone/chorionic gonadotropin receptors in human breast cell lines. Biol Reprod 57:1202-1210.

23. Sun T, Lei ZM, Rao ChV (1997) Novel regulation of the oviductal glycoprotein gene expression by luteinizing hormone in bovine oviductal epithelial cells. Mol Cell Endocrinol 131:97-108.

24. Huang ZH, Lei ZM, Rao ChV (1997) Novel independent and synergistic effects of human chorionic gonadotropin and gonadotropin releasing hormone on the expression of luteinizing hormone alpha-subunit gene in alpha T3 gonadotrope cells. Mol Cell Endocrinol 130:23-31.

25. Han SW, Lei ZM, Rao ChV (1997) Homologous downregulation of luteinizing hormone/chorionic gonadotropin receptors by increasing the degradation of receptor transcripts in human uterine endometrial stromal cells. Biol Reprod 57:158-164.

26. Lei ZM, Rao ChV (1997) Cis-acting elements and trans-acting proteins in the transcriptional inhibition of gonadotropin releasing hormone gene by human chorionic gonadotropin in immortalized hypothalamic GT1-7 neurons. J Biol Chem 272:14365-14371.

27. Tao YX, Lei ZM, Rao ChV (1997) Luteinizing hormone/human chorionic gonadotropin receptors in lactating rat mammary glands. Life Sci 60:1297-1303.

28. Al-Hader AA, Lei ZM, Rao ChV (1997) Neurons from fetal rat brains contain functional luteinizing hormone/human chorionic gonadotropin receptors. Biol Reprod 56:1071-1076.

29. Tao YX, Bao S, Ackermann DM, Lei ZM, Rao ChV (1997) Expression of luteinizing hormone/human chorionic gonadotropin receptor gene in benign prostatic hyperplasia and prostate carcinoma. Biol Reprod 56:67-72.

30. Hu YL, Lei ZM, Rao ChV (1996) Cis-acting elements and trans-acting proteins in the increased transcription of human chorionic gonadotropin/luteinizing hormone receptor gene in choriocarcinoma cells as compared with normal term pregnancy placenta. Endocrinology 137:3897-3905.
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阮克和

“I enjoy being an Ph.D. advisor in the Texas Medical School.”

阮克和 KE-HE RUAN, M.D., Ph.D.

If you were on campus of Fujian Medical University (FMU) late 1980s, I am sure you still would remember a name, Ke-He Ruan. Dr. Ke-He Ruan was the first returning PhD to FMU from oversea (Japan) at that time. I heard his name on radio, I saw his name on various newspapers. His story of hardworking and outstanding achievement was very touching. He became my hero! Somehow my hero disappeared on FMU campus in early 1990s. A decade later, Dr. Rouqing Huang found my hero in USA.

An able man will not disappoint you. Again, Dr. Ruan has made outstanding achievement in USA. Dr. Ruan is currently an Associate Professor of Medicine, Department of Internal Medicine, Vascular Biology Research Center and Hematology Division, University of Texas Health Science Center, and Ph.D. student advisor of the Graduate School of Biomedical Sciences in University of Texas, Health Science Center at Houston and M.D. Anderson Cancer Center.

He is actively participating in research and teaching. His research involves in two major National Institue of Health (NIH, U.S.A.) funded projects. Following is what Dr. Ruan says about his research. The first Project is “Structure and Functions on Prostanoid Receptors (G-protein coupled receptors)’. The long-term goal of this project is to understand how prostanoid receptors mediate human physiological and pathological vascular and hemodynamic processes, including hemostasis, thrombosis and stroke. Prostanoids, including thromboxane (TXA2) and prostaglandin I2 (PGI2) are a family of bioactive oxygenated metabolites of polyunsaturated fatty acids synthesized by vascular smooth muscle and endothelium. TXA2 is a potent stimulator of platelet aggregation and a constrictor of smooth muscle, and has been implicated as a mediator in diseases such as myocardial infarction, stroke and asthma. PGI2 is a potent vasodilator and inhibitor of platelet aggregation, actions essentially opposite to those of TXA2. The functions of TXB2 and PGI2 are mediated by specific cell surface receptors. Eight types of human prostanoid receptors have been defined. They belong to the G protein-coupled receptor family, with seven transmembrane domains and are coupled to different signal transduction systems. However, the structure and function relationship of the TXA2 receptor (TP) and PGI2 receptor (IP) are poorly defined, with little structural information on how the prostanoids specifically recognize their receptors and how the specific signal transduction is achieved by the initial contact of the receptor with G protein. The opposite receptor-mediated actions of TXA2 and PGI2 led us to hypothesize that the two receptors have distinct 3D structures in their extracellular ligand recognition sites, which determine ligand selectivity, and in their intracellular G protein-coupled sites, which determine signal transduction specificity. We further hypothesize that the ligand-recognition sites are formed by multiple extracellular domains. Our initial focus will be on the human TP receptor. The specific aims are to use recombinant receptor mutants, synthetic peptides, peptide antibodies, circular dichroism and 2D nuclear magnetic resonance spectroscopy, molecular modeling and functional assays to: 1) Identify the peptide segments and key residues making up the ligand recognition site(s) of the TP receptor; 2) Determine the 3D structures of the peptides mimicking the extracellular domains of the receptor; 3) Characterize the structures of the TP receptor ligand, and complexes of the ligand with the receptor fragments, and thus build a 3D structural model of the receptor/ligand interaction; and 4) Localize the G protein-coupling site(s) and determine 3D structures of the segments comprising the intracellular domains of the receptor. Results from the proposed studies with the TP receptor will guide later characterization of the IP receptor, will be important for understanding the structure/function relationships of the TP and IP receptors, and will also develop generally useful approaches to solving the 3D structures of these important domains in other prostanoid receptors, and in other G protein-coupled receptors.

The second project is “Structure and Function Studies on Eicosanoid-Synthesizing Cytochrome P450s”. The long-term goal of this project is to understand how the native, membrane-bound structures of two eicosanoid-synthesizing cytochrome P450s, thromboxane A2 synthase (TXAS) and prostaglandin I2 synthase (PGIS), influence their enzyme functions and their coordination with prostaglandin H2 synthase (PGHS), and to understand the membrane topology of mammalian P450 superfamily. TXAS converts prostaglandin H2 (PGH2), produced by PGHS in endoplasmic reticulum (ER) lumen to thromboxane A2 (TXA2) on the cytoplasmic side of the ER. TXA2 is a mediator with potent platelet aggregatory and vasoconstrictive properties. PGIS converts the same substrate, PGH2, to prostaglandin I2 (PGI2), with biological functions opposite to TXA2. TXA2 and PGI2 play important roles in a wide variety of physiological and pathological processes, including hemostasis, atherogenesis, thrombosis and stroke. Our studies have indicated that the large cytoplasmic domain of PGIS is anchored to the ER membrane by a single N-terminal anchor segment similar to that in other microsomal P450s, but different from TXAS, which appears to have two membrane anchor segments. The results also indicate that the PGIS N-terminal membrane anchor near the opening of the substrate access channel affected the enzyme reaction rate. These results led us to hypothesize that PGIS and TXAS have specific substrate-recognition sites in their N-terminal membrane domains, which facilitate substrate access to their active site channels. We also suspected that the helix F/G loop of TXAS and PGIS contains a membrane contact region distinct from the N-termini. PGHS crystallographic studies suggest that their catalytic domains of PGHS are anchored to the ER lumen by helices A-D, and thus directly abutting the substrate channel to the ER membrane. Biosynthesis of TXA2 or PGI2 involves coordination of either TXAS or PGIS with PGHS anchored on the opposite side of the ER membrane. This raises the possibility that the coordination is influenced by the membrane anchors. To test these hypotheses, we propose to analyze and compare the structures and functions of the membrane anchor domains of TXAS, PGIS, PGHS and P450 2C1, using recombinant proteins, synthetic peptides, peptidoliposome, site-specific antibodies, immunocytochemistry, molecular modeling, circular dichroism and 2D nuclear magnetic resonance spectroscopy. The Specific Aims are to: 1) Characterize TXAS and PGIS N-terminal membrane anchor domains which influence the enzyme catalysis, localize the residues important to function and determine the 3D structures of the complex with the interactions between the substrate analog and the membrane domains; 2) Identify membrane contact regions in helix F/G loops of TXAS and PGIS and further define their topology and substrate access channels with respect to the ER membrane; 3) Determine the 3D structure of a synthetic peptide mimicking P450 2C1 N-terminal membrane segment to build a general topology and 3D structural models for microsomal P450s; 4) Determine membrane topology and 3D-solution structure of membrane anchor domains of PGHS-1 and -2 in membrane environment. These studies will provide insights into how the movement of hydrophobic substrates from membrane compartment to enzyme active sites and between the active sites in case of PGHS/PGIS and PGHS/TXAS combinations is accomplished in an efficient manner in the membrane environment. Complete 3D structures of PGIS, TXAS and P450 2C1 N-terminal membrane segments will provide the solution structures in the membrane environment, which complement P450 crystallographic data.

If you want to know more details about Dr. Ruan’s research, please read his representative publications attached at the end.

Dr. Ruan obtained his MD and Ph.D. degrees from FMU and in Medical College of Miyazaki, Japan. He went through postdoctoral training in Department of Biochemistry, Baylor College of Medicine in Houston, TX from 1988-1991. He became an Instructor in 1991 in the Division of Hematology, Department of Internal Medicine, University of Texas Medical School at Houston. He was promoted to Assistant Professor of Medicine in 1994, and to Associate Professor in 2002. As a Principle Investigator (PI) Dr. Ruan currently working on almost two million dollars grants from NIH (RO1 grant and one of NIH PPG grants). He is also a co-investigator for multi-million-dollar NIH grants in his Division. There are 3 postdoctoral fellows and 2 graduates in his lab. Dr. Ruan also has obtained many honorable positions such as service on U.S. national grant review panels (NIH) and international review panels (Taiwan).

Dr. Ruan loves our alma mater, FMU. He is currently a guest professor of FMU, and has trained several postdoctoral fellows for FMU. He is also collaborating with Dr. Bi-Fen Chen, Professor of Pathology, FMU.

If you are interested in his work please contact Dr. Ruan. His address is Department of Internal Medicine, Vascular Biology Research Center and Hematology, University of Texas, Medical School at Houston, 6431 Fannin, Houston, Texas 77030. He can also be reached by phone at 713-500-6769 (office), or by email:kruan@uth.tmc.edu <mailto:kruan@uth.tmc.edu>.

Representative Publications:

Ruan, K. -H., Li, D., Ji, J., Lin, Y. -Z., and Gao, X.: Structural characterization and topology of the second potential membrane anchor region in the thromboxane A2 synthase amino terminal domain. Biochemistry, 37, 822-830, 1998.

Lin, Y.-Z., Wu, K.K. and Ruan, K.-H.: Characterization of secondary structure and membrane interaction of the putative membrane anchor domains of prostaglandin I2 synthase and cytochrome P450 2C1. Arch. Biochem. Biophys. 352, 78-84, 1998.

Lin, Y-Z., Deng, H. and Ruan, K.-H.: Topology of catalytic portion of prostaglandin I2 synthase: Identification by molecular modeling-guided site-specific antibodies. Arch. Biochem. and Biophys. 379, 188-197, 2000.

So, S-P., Li, D. and Ruan, K.-H.: Identification of the substrate-interaction site in the N-terminal membrane anchor segment of thromboxane A2 synthase by determination of its substrate analog conformation changes using high resolution NMR technique. J. Biol. Chem. 275, 40679-40685, 2000.

Ruan, K.-H., So, S-P, Wu, J., Huang, A. and Kung J. Solution structure of second extracellular loop of human thromboxane A2 receptor. Biochemistry, 40, 275-280, 2001.

Deng, W.G., Ruan, K-K, Du, M., Sauders, M., and Wu, K.K. Aspirin and salicylate bind to immunoglobulin heavy-chain binding protein (BiP) and inhibit its ATPase activity in human fibroblasts. FASEB J. 15, Nov. 2001.

Deng, H., Huang A., So, S.-P., Lin, Y.-Z. and Ruan, K.-H. Substrate access channel topology in membrane-bound prostacyclin synthase. Biochem. J., March, 2002.
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