Fish FSH receptors bind LH: how to make the human FSH receptor to be more fishy?

Jan Bogerd, Joke C M Granneman, Rüdiger W Schulz, Henry F Vischer

Research output: Contribution to JournalReview articleAcademicpeer-review


In mammals, the interactions between glycoprotein hormones and their cognate receptors are highly specific; unintended cross-reactivity under normal physiological conditions has not been observed. The interactions between fish gonadotropins and their receptors, on the other hand, appeared to be less discriminatory. For example, the catfish follicle-stimulating hormone (FSH) receptor was highly responsive to both catfish luteinizing hormone (LH) and catfish FSH. Similarly, the FSH receptor of coho salmon bound both salmon FSH and LH. In contrast, LH receptors of both species were found to be rather specific for their cognate LH. This paper intends to summarize the current situation with special emphasis to our comparative structure-function studies that aim at elucidating the molecular basis of ligand selectivity (in mammals) and ligand promiscuity (in fish).

Original languageEnglish
Pages (from-to)34-43
Number of pages10
JournalGeneral and Comparative Endocrinology
Issue number1-2
Publication statusPublished - 15 May 2005


  • Animals
  • Fishes
  • Glycoproteins
  • Humans
  • Luteinizing Hormone
  • Protein Binding
  • Receptors, FSH
  • Receptors, Gonadotropin
  • Receptors, LH
  • Journal Article
  • Review


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