Abstract

The overall objective for this project is to gain an in-depth understanding of the importance of the binding of estrogens, androgens, and corticoids to plasma proteins. Specifically, we are engaged in the isolation of corticosteroid-binding globulin (CBG) from several species and the testosterone estradiol-binding globulin from man. The isolated proteins are being characterized as proteins per se in terms of their chemical and physical characteristics. In addition, detailed studies of their interactions with the steroids which they bind are being examined. In addition to these approaches we are examining the mechanisms by which the concentration in plasma of these proteins is controlled by various endocrine influences. Specifically, we are investigating, at this time, the influence of a host of hormonal factors on the level of hepatic mRNA which is responsible for the translation of CBG in the rat. Similar experiments are planned for the control of the testosterone binding protein of the rabbit.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of Diabetes and Digestive and Kidney Diseases (NIDDK)
Type
Research Project (R01)
Project #
5R01DK028562-08
Application #
3228916
Study Section
Endocrinology Study Section (END)
Project Start
1979-10-01
Project End
1987-08-31
Budget Start
1986-09-01
Budget End
1987-08-31
Support Year
8
Fiscal Year
1986
Total Cost
Indirect Cost

  Institution

Name
St. Luke's-Roosevelt Institute for Health Science
Department
Type
DUNS #
City
New York
State
NY
Country
United States
Zip Code
10019

  Publications

Rosner, W (1990) The functions of corticosteroid-binding globulin and sex hormone-binding globulin: recent advances. Endocr Rev 11:80-91
Nakhla, A M; Khan, M S; Rosner, W (1990) Biologically active steroids activate receptor-bound human sex hormone-binding globulin to cause LNCaP cells to accumulate adenosine 3',5'-monophosphate. J Clin Endocrinol Metab 71:398-404
Khan, M S; Rosner, W (1990) Histidine 235 of human sex hormone-binding globulin is the covalent site of attachment of the nucleophilic steroid derivative, 17 beta-bromoacetoxydihydrotestosterone. J Biol Chem 265:8431-5
Hryb, D J; Khan, M S; Romas, N A et al. (1990) The control of the interaction of sex hormone-binding globulin with its receptor by steroid hormones. J Biol Chem 265:6048-54
Maitra, U S; Khan, M S; Zhang, X H et al. (1990) The rat hepatic corticosteroid-binding globulin receptor: distinction from the asialoglycoprotein receptor. Endocrinology 127:278-84
Khan, M S; Hryb, D J; Hashim, G A et al. (1990) Delineation and synthesis of the membrane receptor-binding domain of sex hormone-binding globulin. J Biol Chem 265:18362-5
Nakhla, A M; Khan, M S; Rosner, W (1988) Induction of adenylate cyclase in a mammary carcinoma cell line by human corticosteroid-binding globulin. Biochem Biophys Res Commun 153:1012-8
Singer, C J; Khan, M S; Rosner, W (1988) Characteristics of the binding of corticosteroid-binding globulin to rat cell membranes. Endocrinology 122:89-96
Strain, G W; Zumoff, B; Miller, L K et al. (1988) Effect of massive weight loss on hypothalamic-pituitary-gonadal function in obese men. J Clin Endocrinol Metab 66:1019-23
Rosner, W; Hryb, D J; Khan, M S et al. (1988) Are corticosteroid-binding globulin and sex hormone-binding globulin hormones? Ann N Y Acad Sci 538:137-45

Showing the most recent 10 out of 12 publications