Isolation of bovine follicular fluid inhibin of about 32 kDa

Fukuda, Masaki; Miyamoto, Kaoru; Hasegawa, Yoshihisa; Nomura, Mitsuo; Igarashi, Masao; Kangawa, Kenji; Matsuo, Hisayuki

doi:10.1016/0303-7207(86)90105-x

Cited by 116 publications

(38 citation statements)

References 13 publications

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“…The molecular weight of inhibin and its subunits after reduction agrees well with the reports on purified 32 kDa ovarian inhibin (Ling et al, 1985;Miyamoto et al, 1985;Rivier et al, 1985;Fukuda et al, 1986;Robertson et al, 1986;Leverha et al, 1987). The amino acid sequence which was obtained after combination of the data for the two inhibin preparations shows that rat Sertoli cell inhibin is an ap-B dimer.…”

Section: Discussionsupporting

confidence: 81%

Inhibin in immature rat Sertoli cell conditioned medium: A 32 kDa αβ-B dimer

Grootenhuis

Timmerman

Hordijk

et al. 1990

Molecular and Cellular Endocrinology

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Section: Discussionsupporting

confidence: 81%

Inhibin in immature rat Sertoli cell conditioned medium: A 32 kDa αβ-B dimer

Grootenhuis

Timmerman

Hordijk

et al. 1990

Molecular and Cellular Endocrinology

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“…These are likely to correspond to the higher molecular weight precursor forms of inhibin A, in addition to fully processed 32 kDa inhibin A, as previously described in porcine (Miyamoto et al 1986) and bovine follicular fluid (FF; Sugino et al 1992). Early studies have demonstrated the existence of high concentrations of a 26 kDa-free a subunit (pro-aC) in bovine FF (Knight et al 1989, Robertson et al 1989, Sugino et al 1989 and in the circulation (Knight et al 1989).…”

Section: Discussionmentioning

confidence: 99%

“…Moreover, interpretation of the inhibin profiles obtained by the inhibin immunoassays used in the above studies (Hasegawa et al 1988, Mukai et al 1989, Trout et al 1992, Knox et al 2003 involves uncertainty. The ovary synthesizes inhibin dimers (inhibin A, a dimer of a and b A subunits; and inhibin B, a dimer of a and b B ) that have FSH-suppressing activity (Ling et al 1985, Miyamoto et al 1985, Rivier et al 1985, Robertson et al 1985, Fukuda et al 1986; it also produces substantial amounts of free a subunits of inhibin that have no FSH-suppressing activity (Knight et al 1989, Robertson et al 1989, Sugino et al 1989. However, because the assays used in previous studies were based on antisera directed against the a subunits of inhibin (Hasegawa et al 1988, Mukai et al 1989, Trout et al 1992, Knox et al 2003, they did not discriminate the dimeric inhibins from the free a subunits.…”

Section: Introductionmentioning

confidence: 99%

Peripheral concentrations of inhibin A, ovarian steroids, and gonadotropins associated with follicular development throughout the estrous cycle of the sow

Noguchi¹,

Yoshioka²,

Itoh³

et al. 2010

Reproduction

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We investigated changes in peripheral concentrations of inhibin A, total inhibin, steroids, and gonadotropins throughout the intact estrous cycle of the sow in relation to ovarian changes determined by daily transrectal ultrasonography. All visible follicles of 3 mm or more in diameter were classified as small (R3 and !6 mm) or large (R6 mm). Follicular recruitment was identified in two periods of the cycle: one from the late luteal to the follicular phase, characterized by an increase in the number of small follicles followed by the appearance of large follicles; and another during the early luteal phase, consisting only of increased numbers of small follicles. Plasma concentrations of inhibin A increased (P!0.05), coinciding with the two periods of follicle emergence. Estradiol (E 2 ) levels increased (P!0.05) during the follicular phase, but not during the early luteal phase. An inverse relationship (P!0.01) between the patterns of inhibin and FSH concentrations was noted around the two periods of follicle emergence, but there was no relationship (PR0.1) between the patterns of plasma E 2 and FSH during the early luteal phase. In conclusion, measurement of plasma inhibin A levels combined with ultrasonographic examination of the ovaries revealed two periods of synchronous follicular growth during the sow's estrous cycle. The results strongly suggest that inhibin A functions as a negative feedback regulator of FSH secretion throughout the estrous cycle, whereas E 2 appears to influence FSH secretion only during the follicular phase.Reproduction (2010) 139 153-161

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“…However, the search for the elusive inhibin did not succeed until 1985, when two closely related glycoproteins of apparent Mr 32,000, named inhibins A and B, were isolated from porcine ovarian follicular fluid (4-6). Subsequently, a similar Mr 32,000 inhibin was also isolated from bovine ovarian follicular fluid (7,8). Each inhibin was found to be composed of a common Mr 18,000 glycosylated a subunit linked by interchain disulfide bond(s) to either a PA subunit ofMr 14,700 to yield inhibin A or a PB subunit of Mr 14,000 to form inhibin B; the two 13 subunits were closely related but distinct from each other (4).…”

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confidence: 99%

Isolation and partial characterization of follistatin: a single-chain Mr 35,000 monomeric protein that inhibits the release of follicle-stimulating hormone.

Ueno

Ling

Ying

et al. 1987

Proc. Natl. Acad. Sci. U.S.A.

426

167

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A Mr 35,000 protein with follicle-stimulating hormone release-inhibitory activity was isolated from porcine ovarian follicular fluid by heparin-Sepharose affinity chromatography, gel fitration on Sephacryl S-200, and multiple steps of high-performance liquid chromatography. The isolated molecule is highly enriched in cysteines and is composed of a single polypeptide chain. In addition, it has no sequence homology with the previously characterized follicular fluid inhibins, which are heterodimeric proteins of Mr 32,000 with follicle-stimulating hormone release-inhibiting activity. This protein specifically inhibits the basal secretion of follicle-stimulating hormone, but not that of luteinizing hormone, in the rat anterior pituitary monolayer culture system with a halfmaximal effective dose of 2.5-6.0 ng/ml. Another form of the molecule of Mr 32,000 present in much lower concentration in follicular fluid was also isolated. It may differ from the Mr 35,000 form in glycosylation or carboxyl-terminal truncation. We suggest that this compound be called "follistatin" to signify its structural difference from inhibin.Secretion of pituitary follicle-stimulating hormone (FSH) is principally regulated by the hypothalamic hypophysiotropic gonadotropin-releasing hormone and gonadal steroids (1). But for many years the existence of a nonsteroidal, watersoluble factor from the gonad that feeds back on the pituitary specifically to suppress the secretion of FSH has been advocated by many researchers (2); the name "inhibin" was coined in 1932 to describe such a factor (3). However, the search for the elusive inhibin did not succeed until 1985, when two closely related glycoproteins of apparent Mr 32,000, named inhibins A and B, were isolated from porcine ovarian follicular fluid (4-6). Subsequently, a similar Mr 32,000 inhibin was also isolated from bovine ovarian follicular fluid (7,8). Each inhibin was found to be composed of a common Mr 18,000 glycosylated a subunit linked by interchain disulfide bond(s) to either a PA subunit ofMr 14,700 to yield inhibin A or a PB subunit of Mr 14,000 to form inhibin B; the two 13 subunits were closely related but distinct from each other (4). The common a subunit can exist also in a larger molecular form of Mr 44,000 and, in combination with the 13 subunit of inhibin A, can form an inhibin of Mr 56,000 (9).Using partial amino acid sequence information, the messages encoding the a, PA, and PB subunits of porcine inhibin were cloned from an ovarian cDNA library (10) as were the a and PA subunits of bovine inhibin (11). DNA sequence analyses showed that all of the subunits were initially synthesized as large precursor proteins with the mature subunits residing at the carboxyl-terminal portion of the precursors. Surprisingly, the two P subunits, besides being homologous to each other, were found to be structurally related to a homodimeric protein, transforming growth factor ,3, which has totally different biological activities (10). Moreover, in addition to the inhibins, two FSH-releas...

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Isolation of bovine follicular fluid inhibin of about 32 kDa

Cited by 116 publications

References 13 publications

Inhibin in immature rat Sertoli cell conditioned medium: A 32 kDa αβ-B dimer

Inhibin in immature rat Sertoli cell conditioned medium: A 32 kDa αβ-B dimer

Peripheral concentrations of inhibin A, ovarian steroids, and gonadotropins associated with follicular development throughout the estrous cycle of the sow

Isolation and partial characterization of follistatin: a single-chain Mr 35,000 monomeric protein that inhibits the release of follicle-stimulating hormone.

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