Abstract
Transforming growth factor β1 (TGF-β1) is a polypeptide growth factor with various biological activities. Recent studies have shown that this growth factor and they receptors are expressed in human Leydig cells, Sertoli cells, spermatogonia, spermatocytes and sperm cells after birth, and are involved in the endocrine regulation of spermatogenesis. However, there is no report on the expression of TGF-β in human embryonic testis. TGF-β1 is a peptide growth factor widely distributed in germ cells at various levels in the testis, regulating the function of the testes and maintaining the stability of the testis environment by acting on various cells. This review summarizes the research progress of TGF-β1 in human testis.
Highlights
Testicular formation and spermatogenesis is a delicate and complex process
It is well known that tight junctions formed by adjacent Sertoli cells are a major component of the blood testis barrier and it plays an important role in maintaining the microenvironment of spermatogenesis in the testes
Transforming growth factor β1 (TGF-β1) is mainly mediated by type 1 receptors, which promotes the proliferation of extracellular matrix, activates cells’ PAL-1, and coordinates with PAL-1 secreted by the Sertoli cells (Zhang et al, 2014)
Summary
Testicular formation and spermatogenesis is a delicate and complex process. There are complex cellular pathways between various cells, and the secretion and action of various hormones are complicated. TGF-β is first TβRII binding undergoes non-ligand-dependent autophosphorylation activation to form a complex, at which point TβRII phosphorylation kinase is activated, TβRI recognizes and binds to this compound, and is activated by phosphorylation of TβRII phosphorylation kinase, through such a process Initiation of intracellular signal generation. It is generally believed that in TGF-β-induced signal transduction, TGF-β first directly binds to TβRII to form a complex, TGF-β conformation changes, is recognized by TβR-1 and binds to form TβRII-TGF-β -TβRI trimer complex, TβRI in the complex is phosphorylated by TβRII, causing its substrate to amplify the signal and further downstream, which is the most important way of binding the receptor to the ligand, that is the mediated recruitment method (Nayeem & Deep 2014). When these two receptors are simultaneously expressed in the cell and present on the cell membrane, their affinity with the ligand is greatly enhanced (Sabbineni et al 2018)
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