# FSH/FSH-RECEPTOR STRUCTURE-FUNCTION RELATIONSHIPS

> **NIH NIH R01** · WADSWORTH CENTER · 1994 · $150,611

## Abstract

The present proposal extends previous biochemical and immunochemical            
work aimed at understanding the FSH/FSH-receptor interaction.  Data             
collected during the previous grant period has identified specific              
regions of both hFSH subunits (hFSHalpha, hFSHbeta) which by these              
methods are involved in FSH-receptor binding and FSH-subunit contact.           
The first objective of the present proposal is to prepare mutant hFSH           
which has been substituted with alanine at residues within the                  
sequences identified as putative receptor binding sites.  The                   
operating hypothesis is that amino acids within sequence hFSHbeta -             
(33-53) and hFSHalpha- (73-92) are in part, the assembled receptor              
binding site of hFSH.  Mutant hFSH will be tested to determine if the           
mutation causes an alteration in receptor binding and activation.               
The second objective is to mutate hFSH within sequences which have              
been identified as subunit association sites.  Data collected during            
the previous grant period have identified sequences hFSHbeta- (81-              
100) and hFSHalpha- (33-58) as containing amino acids which                     
participate n subunit association to form heterodimeric hFSH.  The              
hypothesis is that mutation of amino acids involved in subunit                  
association will result in altered ability of subunits to form                  
heterodimeric hFSH.  Whether or not the mutated hFSH subunits will              
form heterodimers will be assessed.  The third objective is corollary           
to the first two objectives.  The applicant proposes to define the              
extracellular FSH binding domain of the FSH receptor.  Recombinant              
rat FSH receptor will then be used to immunize mice to produce                  
antibodies against the receptor.  Monoclonal anti-receptor antibodies           
which block binding of hFSH to FSH-receptor will then be epitope                
mapped using FSH-receptor synthetic peptides.  This will allow                  
determination of specific residues which comprise in part the FSH               
binding site of the FSH-receptor.                                               
                                                                                
The long term goals are to understand the molecular (structural)                
basis of how human follicle stimulating hormone (hFSH) interacts with           
its receptor and  how FSH subunits associate to form biologically               
active heterodimer.  This understanding will contribute to the                  
knowledge necessary to an FSH or FSH-receptor based, contraceptive              
vaccine.  Additionally, perhaps a second generation of hormones that            
are more potent (agonistic) than hFSH or can inhibit (antagonist)               
hFS...

## Key facts

- **NIH application ID:** 2197654
- **Project number:** 5R01HD018407-09
- **Recipient organization:** WADSWORTH CENTER
- **SAM.gov UEI:** LQK1DD1EYZK9
- **Principal Investigator:** DIAS JAMES A
- **Activity code:** R01 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 1994
- **Award amount:** $150,611
- **Award type:** 5
- **Project period:** 1988-04-01 → 1996-02-28

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/2197654

## Citation

> US National Institutes of Health, RePORTER application 2197654, FSH/FSH-RECEPTOR STRUCTURE-FUNCTION RELATIONSHIPS (5R01HD018407-09). Retrieved via MORVS 2026-10-25 from https://api.morvs.ai/grant/nih/2197654. Licensed CC0.

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