Bibliographie

Structure of the human melanin concentrating hormone mRNA

eng

Presse F ; Nahon JL ; Fischer WH ; Vale W ;

Mol Endocrinol vol. 4 (4)   pp. 632-7, Avr 1990

Clayton Foundation for Peptide Biology Laboratories, Salk Institute for Biological Studies, San Diego, California 92138-9216.



The melanin-concentrating hormone (MCH) is a cyclic neuropeptide which induces skin paling and may be involved in the control of the pituitary adrenal axis in teleost fishes. We have recently cloned and characterized the salmon and rat MCH mRNAs and we report in the present paper the cloning and sequencing of the human counterpart. The deduced human MCH (hMCH) precursor is 165 amino acids long and as for rat and salmon, encodes the MCH peptide at the C-terminus. The human and rat MCH precursors are very similar to one another but differ extensively from the salmon counterpart. Strong sequence conservation was found in the regions of mammalian prohormones encoding the novel putative neuropeptides named NGE and NEI which we had originally identified in the rat MCH precursor. Furthermore, sequence identities, with perhaps functional implications, were found among the MCH, human ANF, and aplysia peptide A hormone precursors.


Amino acid sequence ;  Animal ;  Aplysia: genetics ;  Atrial Natriuretic Factor: genetics ;  Base Sequence ;  Comparative Study ;  DNA: genetics ;  Gene Library ;  Human ;  Hypothalamus ;  Melanins: genetics ;  Molecular Sequence Data ;  Neuropeptides: genetics ;  Pituitary Hormones: genetics ;  Protein Precursors: genetics ;  Rats: genetics ;  Salmon: genetics ;  Sequence Alignment ;  Sequence Homology,Nucleic Acid ;  Species Specificity ;  Support,Non-U.S.Gov't ;  Support,U.S.Gov't,Non-P.H.S. ;  Support,U.S.Gov't,P.H.S. ;  43140 ; 

 


 
     
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