Primary amino acid sequence of follicle-stimulating hormone from human pituitary glands. I. alpha subunit.

The three substances now used to stimulate the gonads in infertility are human follicle stimulating hormone (HFSH) obtained mainly from post-menopausal urine, but also from human pituitary glands, human chorionic gonadotrophin (HCG) extracted from the urine of pregnant women, and clomiphene (Clomid - Merrell), a synthetic compound which we reviewed in 1967.1

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Intracellular Retention of the Corticotrophin-releasing Hormone (CRH) Precursor Within COS-7 Cells

Journal of Histochemistry & Cytochemistry ◽

10.1177/002215549804601012 ◽

1998 ◽

Vol 46 (10) ◽

pp. 1193-1197 ◽

Cited By ~ 1

Author(s):

Marcelo J. Perone ◽

Simon Windeatt ◽

Ewan Morrison ◽

Andy Shering ◽

Peter Tomasec ◽

...

Keyword(s):

Amino Acid ◽

Golgi Apparatus ◽

Amino Acid Sequence ◽

Protein Secretion ◽

Intracellular Trafficking ◽

Secretory Pathway ◽

Intracellular Localization ◽

Primary Amino Acid Sequence ◽

Releasing Hormone ◽

Primary Amino

We investigated the intracellular localization of CRH in transiently transfected COS-7 cells expressing the full-length rat corticotropin-releasing hormone (CRH) precursor cDNA. CRH synthesized by transfected COS-7 cells is mainly stored intracellularly. In contrast, CHO-K1 cells expressing the same CRH precursor stored and released equal amounts of immunoreactive (IR)-CRH. Ultrastructural analysis revealed that CRH is stored in electron-dense aggregates in the RER of transiently transfected COS-7 cells and does not migrate into the Golgi apparatus. On the basis of the different intracellular localization, storage, and release of CRH in COS-7 and CHO-K1 cells, we hypothesize that the intracellular trafficking of CRH within the constitutive secretory pathway for protein secretion not only depends on its primary amino acid sequence but might also be influenced by intracellular conditions or factors.

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Amino acid sequence and the cellular location of the Na+-dependent d-glucose symporters (SGLT1) in the ovine enterocyte and the parotid acinar cell

Biochemical Journal ◽

10.1042/bj3120293 ◽

1995 ◽

Vol 312 (1) ◽

pp. 293-300 ◽

Cited By ~ 28

Author(s):

P S Tarpey ◽

I S Wood ◽

S P Shirazi-Beechey ◽

R B Beechey

Keyword(s):

Plasma Membrane ◽

Amino Acid ◽

Amino Acid Sequence ◽

Acinar Cell ◽

Acinar Cells ◽

Amino Acid Sequences ◽

Primary Amino Acid Sequence ◽

Parotid Acinar Cells ◽

Parotid Acinar Cell ◽

Primary Amino

The Na(+)-dependent D-glucose symporter has been shown to be located on the basolateral domain of the plasma membrane of ovine parotid acinar cells. This is in contrast to the apical location of this transporter in the ovine enterocyte. The amino acid sequences of these two proteins have been determined. They are identical. The results indicated that the signals responsible for the differential targeting of these two proteins to the apical and the basal domains of the plasma membrane are not contained within the primary amino acid sequence.

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