# HEAT-SHOCK-LIKE GENE REGULATION BY REPRODUCTIVE HORMONES

> **NIH NIH R01** · MOUNT SINAI SCHOOL OF MEDICINE OF CUNY · 1993 · $126,077

## Abstract

These studies will examine regulation of heat-shock-70-like protein
(hsp70) isoforms and mRNAs by reproductive hormones.  Since the
hsp70 family comprises several highly related but distinct beat-
shock-induced and constitutive gene products, high-resolution
biochemical techniques (2-D gels, Western, slot, and Northern
blots) and high-resolution cytochemical techniques (in situ
hybridization and immunocytochemistry) will be used in conjunction
with 4 antibody and 2 cDNA probes assembled for this project, each
with distinct specificities.  Heat-shock gene products are induced
during gametogenesis in ovaries, testes, and even sporulation, and
during early embryonic development; inappropriate expression of
heat-shock proteins can lead to developmental defects.  In
addition, oncogenes induce hsp70 gene products and these products
are elevated in transformed cells.  Some hsp70 isoforms facilitate
transport of secreted proteins into the endoplasmic reticulum and
remove clathrin from coated vesicles, suggesting a role in
secretion, but the regulation and role of hsp70 gene products in
reproduction are not understood.  However, estrogen and prolactin
induce hsp70 mRNA.  Furthermore, the most prominent estrogen-
induced protein in ventromedial hypothalamus (EI70) and LHRH-
induced protein (LHRH70) in pituitary is apparently the same hsp70-
like isoform.  Thus hsp70 isoforms may be generally involved in
reproductive neuroendocrine processes.

(I)  The relationship between EI70, LHRH70 specific hsp70 isoforms
will be studied using ATP binding, co-migration, immunoblots,
peptide maps, and protein sequencing.

(II)  The induction of hsp70 isoforms and mRNA by estrogen, LHRH,
prolactin, and prostaglandin E2 in brain, pituitary, and uterus
will be examined using 2-D gels, immunocytochemistry, Northern and
slot blots, and in situ hybridization, and correlated with
regulation of reproductive functions.

(III)  The subcellular localization of hsp70 proteins after
hormonal stimulation will be assessed with immunocytochemistry and
subcellular fractionation, since localization of hsp70 isoforms is
regulated by beat-shock and during the cell cycle.  (IV) If time
permits, hsp24 and hsp108, whose mRNAs are regulated by
reproductive steroids, will be studied similarly using available
probes.  These studies may provide better understanding of the
reproductive regulation of heat-shock proteins and their functional
relation to reproductive cancers, birth defects, and fertility.

## Key facts

- **NIH application ID:** 2199631
- **Project number:** 7R01HD025543-05
- **Recipient organization:** MOUNT SINAI SCHOOL OF MEDICINE OF CUNY
- **Principal Investigator:** CHARLES V MOBBS
- **Activity code:** R01 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 1993
- **Award amount:** $126,077
- **Award type:** 7
- **Project period:** 1989-05-01 → 1995-04-30

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/2199631

## Citation

> US National Institutes of Health, RePORTER application 2199631, HEAT-SHOCK-LIKE GENE REGULATION BY REPRODUCTIVE HORMONES (7R01HD025543-05). Retrieved via MORVS 2026-10-25 from https://api.morvs.ai/grant/nih/2199631. Licensed CC0.

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