Prolactin receptor

Nagasawa, Hiroshi; Sakai, Senkiti; Banerjee, M. R.

doi:10.1016/0024-3205(79)90220-0

Cited by 36 publications

(5 citation statements)

References 72 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The role of prolactin in the growth and development of experimental mammary tumours is well established (Welsch and Nagasawa, 1977) but its importance in human breast cancer is less well understood. Prolactin, like other polypeptide hormones, initiates its action by binding to cell surface receptor sites on target cells (Nagasawa et al, 1979), so it is likely that prolactin-induced responses of cells are dependent upon prolactin-receptor interactions. The determination of prolactin receptors in tissues may therefore serve as an indicator of responsiveness to prolactin, which could have therapeutic implications in the management of human breast cancer.…”

mentioning

confidence: 99%

The localization of prolactin binding sites in human breast tissue

Dhadly¹,

Walker²

1983

Intl Journal of Cancer

View full text Add to dashboard Cite

An immunohistochemical method involving the application of purified human prolactin and a specific antiserum to human prolactin, followed by the peroxidase-anti-peroxidase immunoperoxidase technique, has been used to detect prolactin binding in benign and malignant human breast tissue. The use of fresh, frozen material has been found to be essential. Prolactin binding has been shown to be a consistent feature of benign breast tissue but a variation within samples has been noted which is irrespective of hyperplastic changes. Fifty six percent of breast carcinomas gave a positive reaction but heterogeneity of binding has been shown to be a significant feature. A relationship between the presence and extent of prolactin binding and good histological differentiation of the tumours has been noted. It is concluded that immunohistochemistry is a suitable method for the demonstration of prolactin binding sites in human breast tissue and can provide useful information with regard to tumour heterogeneity.

show abstract

mentioning

confidence: 99%

The localization of prolactin binding sites in human breast tissue

Dhadly¹,

Walker²

1983

Intl Journal of Cancer

View full text Add to dashboard Cite

show abstract

“…Prolactin (PRL) mediates its diverse physiologic actions by interacting with a membrane receptor of the target tissue (Nagasawa et al, 1979;Shiu and Friesen, 1980). The interaction between PRL and the receptor is a chemical reaction, and the PRL binding to the receptor is influenced by ions and their ionic strength (Shiu and Friesen, 1974;Haro and Talamantes, 1985).…”

mentioning

confidence: 99%

Interaction Between Prolactin and Rabbit Mammary Prolactin Receptor in the Presence of Environment-Modifying Agents.

Sakai

Suzuki

1989

Endocrinol Japon

Self Cite

View full text Add to dashboard Cite

The binding assay of prolactin (PRL) to the receptor in the rabbit mammary gland was carried out with varying concentrations of NaCl, KCl, CaCl2, MgCl2, glycerol, glucose, sucrose and urea. The agents did not affect the binding capacity. The ionic bond-breaking agents (NaCl and KCl) had little effect on changes in the association rate constant (k+1) of PRL binding to the receptor and the dissociation rate constant (k_1) of bound PRL. The inclusion of other agents changed the k+1 and the k-1. Among the agents examined, chaotropic salts (CaCl2 and MgCl2) inhibited the binding of PRL greatly, and were the most effective in decreasing the k+1. Both hydrogen-and hydrophobic bonds are involved in the interaction between PRL and the receptor.The data suggest that hydrophobic bonding is primarily an important force participating in the binding of PRL to its receptor.

show abstract

“…These observations contrast with those made using rabbit and mouse mammary gland, when progestin treatment resulted in a decrease in PRLR-binding activity. In DMBAinduced rat mammary tumours progestins had no effect and androgens reduced PRLR-binding activity (reviewed by Nagasawa et al, 1979).…”

Section: Discussionmentioning

confidence: 99%

Androgen regulation of prolactin‐receptor gene expression in MCF‐7 and MDA‐MB‐453 human breast cancer cells

Ormandy

Kelly

Sutherland

1992

Intl Journal of Cancer

View full text Add to dashboard Cite

Lactogenic hormones which bind to the PRLR are likely to be growth-stimulatory in human breast-cancer cells. Oestrogen and progesterone control cellular expression of the PRLR; however, elevated androgen levels in some breast-cancer patients raised the possibility that androgens may also influence breast-cancer sensitivity to lactogenic hormones. This study investigated whether androgens could affect expression of the PRLR in the MCF-7 breast-cancer cell line. PRLR binding activity was increased approximately 2-fold by treatment for 24 hr with 10 nM R1881, TEST, DHT, MPA and ORG 2058. Northern analysis indicated that DHT also increased the level of PRLR mRNA. The antiprogesterone, RU 38486, displaced tritiated ORG 2058 binding but not tritiated DHT binding to MCF-7 cells; it completely antagonized ORG 2058 and partially antagonized R1881 induction of the PRLR, but had no effect on induction by DHT. The anti-androgen, RU 23908, displaced tritiated DHT binding but not tritiated ORG 2058 binding, and antagonized DHT and R1881 induction of PRLR but not induction of the PRLR by ORG 2058. These data indicated that ORG 2058 acting via the PR and DHT acting via the AR were able to induce PRLR expression in MCF-7 cells. In MDA-MB-453 cells, which express the AR but not the ER or PR, DHT and R1881 increased PRLR binding to 150% of control values at 0.1 nM. ORG 2058 was ineffective, demonstrating androgen induction of PRLR in the absence of PR and ER. These data indicate that PRLR can be regulated by androgens in MCF-7 and MDA-MB-453 human breast-cancer cells.

show abstract

Prolactin receptor

Cited by 36 publications

References 72 publications

The localization of prolactin binding sites in human breast tissue

The localization of prolactin binding sites in human breast tissue

Interaction Between Prolactin and Rabbit Mammary Prolactin Receptor in the Presence of Environment-Modifying Agents.

Androgen regulation of prolactin‐receptor gene expression in MCF‐7 and MDA‐MB‐453 human breast cancer cells

Contact Info

Product

Resources

About