The Action of Calcitonin on the TM<sub>4</sub> Sertoli Cell Line and on Rat Sertoli Cell‐Enriched Cultures

Wiley - Tập 10 Số 4 - Trang 321-331 - 1989
Atif M. Nakhla1, Jennie P. Mather1, Olli A. Jänne1, C. Wayne Bardin1
1Population Council, New York, New York.

Tóm tắt

The effects of synthetic salmon calcitonin on primary Sertoli cell‐enriched cultures and on an established cell line (TM4 cells, derived from immature mouse Sertoli cells) were studied. Synthetic salmon calcitonin stimulated the conversion of [3H]adenine to [3H]cyclic AMP in both cell systems. In addition, this peptide stimulated the secretion of rABP in primary Sertoli cellenriched cultures prepared from rat testis. Calcitonin also increased the total concentration of both androgen and estrogen receptors in TM4 cells. Because cAMP analogs decreased androgen and estrogen receptor concentrations, the effect of calcitonin on sex steroid receptors may not be mediated by its effect on cyclic AMP in these cells. The possibility that the action of synthetic salmon calcitonin on the receptors might be mediated by a change in cellular Ca2+ was investigated. Lowering extracellular Ca2+ concentrations from 1.5 mM to less than 0.01 mM markedly reduced the concentration of androgen and estrogen receptors; restoration of Ca2+ to 1.5 mM returned receptor levels to normal. When the receptor concentrations were decreased by lowering extracellular Ca2+ concentrations to 0.5 mM, treatment with the calcium ionophore, A23187, restored receptor levels to normal. Although the calcium channel blocker, verapamil, decreased receptor levels, calcitonin partially counteracted its effect. Trifluoperazine, an inhibitor of calmodulin, also diminished androgen and estrogen receptor levels in the cytosol of TM4 cells. It was concluded that calcitonin stimulates the formation of cyclic AMP and the secretion of rABP by Sertoli cells. This peptide also increases the concentration of androgen and estrogen receptors, possibly by a mechanism that is, in part, Ca2+‐mediated. These results, along with those on Leydig cells, suggest that calcitonin could be a regulator of testicular function.

Từ khóa


Tài liệu tham khảo

10.1016/0022-4731(80)90277-0

Bodwin JS, 1978, Inverse relation between estrogen receptors and cyclic adenosine 3î5‐monophosphate binding proteins in hormone‐dependent mammary tumor regression due to dibutyrl cyclic adenosine 3î:5î monophosphate treatment or ovariectomy, Cancer Res, 38, 3410

10.1016/0003-2697(76)90527-3

10.1210/endo-94-3-746

10.1016/S0039-128X(75)80011-0

10.1210/endo-114-4-1196

10.1016/0003-2697(79)90131-3

Chausmer A., 1980, Identification of testicular cell plasma membrane receptors for calcitonin, J Lab Clin Med, 96, 933

10.1126/science.6281881

10.1083/jcb.91.1.195

10.1210/endo-111-5-1671

10.1073/pnas.80.9.2486

Franchi E., 1983, Destabilizing effect of a calmodulin blocker on inter‐Sertoli junction arrangement, J Cell Biol, 97, 17a

10.1126/science.635573

10.1016/0022-4731(83)90411-9

10.1210/endo-111-3-833

10.1016/0022-4731(83)90244-3

10.1095/biolreprod27.1.233

10.1210/jcem-38-3-500

10.1016/0003-2697(80)90165-7

Larrea F., 1981, Origin of the heavy and light promotors of androgen‐binding protein from the rat testis, J Biol Chem, 256, 12566, 10.1016/S0021-9258(18)43312-1

10.1210/endo-109-4-1212

10.1038/302790a0

10.1016/0304-4165(80)90317-7

10.1095/biolreprod23.1.243

Mather JP, 1984, Methods in molecular and cell biology, 100

10.1146/annurev.ph.42.030180.000423

10.1038/285073a0

10.1016/0303-7207(80)90052-0

10.1111/j.1749-6632.1982.tb23162.x

10.1016/0022-4731(83)90404-1

10.1073/pnas.81.19.5921

10.1095/biolreprod28.3.528

10.3109/07435807709073919

10.1021/bi00554a006

10.1210/endo-115-1-121

Nakhla AM, 1989, The actions of calcitonin on the TM3 Leydig cell line and on rat Leydig cell‐enriched cultures, J Androl, 10, 000

Ng KW, 1983, Calcitonin effects on growth and on selective activation of type II isoenzyme of cyclic adenosine 3î:5î‐monophosphate‐dependent protein kinase in T 47D human breast cancer cells, Cancer Res, 43, 794

OnoT. KoideY. AraiY. YamashitaK.Calmodulin binding protein in rat testis: characterization and the effects of surgical cryptorchidism.Program of the 7th International Congress of Endocrinology Abst. No. 1424. Quebec Canada1984;972.

10.1210/jcem-53-2-318

10.1210/endo-118-1-383

10.1016/0022-4731(77)90211-4

10.1210/endo-113-6-2284

10.1016/0022-4731(84)90186-9

Salomon Y., 1979, Adenylate cyclase assay, Adv Cyclic Nucleotide Protein Phosphorylation Res, 10, 35

10.1016/0022-4731(81)90165-5

10.1095/biolreprod23.3.495

10.1111/j.1749-6632.1977.tb29406.x

10.1016/S0076-6879(75)36021-7

Sherman MR, 1983, Structure dissociation and proteolysis of mammalian steroid receptors. Multiplicity of glucocorticoid receptor forms and proteolytic enzymes in rat liver and kidney cytosols, J Biol Chem, 258, 10366, 10.1016/S0021-9258(17)44466-8

Sherman MR, 1985, Mechanisms and clinical aspects of steroid hormone resistance, 150

10.1073/pnas.80.3.760

Bohemen CG, 1983, Control by calcium ions of steroid binding to the glucocorticoid receptor, Mol Physiol, 4, 95

10.1021/bi00543a014

10.1210/endo-111-1-1

10.1016/0022-4731(80)90200-9

10.1016/0022-4731(83)90099-7

10.1021/bi00393a046

Wilson EM, 1976, Binding properties of androgen receptors. Evidence for identical receptors in rat testis, epididymis and prostate, J Biol Chem, 251, 5620, 10.1016/S0021-9258(17)33103-4

10.1073/pnas.78.12.7565

10.1016/0022-4731(82)90202-3