Pilus-facilitated adherence of Neisseria meningitidis to human epithelial and endothelial cells: modulation of adherence phenotype occurs concurrently with changes in primary amino acid sequence and the glycosylation status of pilin

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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CD156 (Human ADAM8): Expression, Primary Amino Acid Sequence, and Gene Location

Genomics ◽

10.1006/geno.1997.4607 ◽

1997 ◽

Vol 41 (1) ◽

pp. 56-62 ◽

Cited By ~ 74

Author(s):

Kazuhiro Yoshiyama ◽

Yasunori Higuchi ◽

Masashi Kataoka ◽

Keiko Matsuura ◽

Shunsuke Yamamoto

Keyword(s):

Amino Acid ◽

Amino Acid Sequence ◽

Gene Location ◽

Primary Amino Acid Sequence ◽

Primary Amino

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New Delhi metallo-β-lactamase (NDM)

The Biochemist ◽

10.1042/bio03703018 ◽

2015 ◽

Vol 37 (3) ◽

pp. 18-21

Author(s):

Hao Yang ◽

Michael W. Crowder

Keyword(s):

Antibacterial Activity ◽

Amino Acid ◽

Amino Acid Sequence ◽

Substrate Preference ◽

New Delhi ◽

Primary Amino Acid Sequence ◽

Substrate Specificities ◽

Clinical Variants ◽

Primary Amino ◽

Multiple Variants

Metallo-β-lactamases (MBLs) are a class of Zn(II)-containing enzymes that hydrolyse the β-lactam bond in β-lactam-containing antibiotics, resulting in products that no longer exhibit antibacterial activity. Currently, there are 29 known MBLs (not including variants), and these enzymes have been classified on the basis of primary amino acid sequence and functionality into three or four classes (see www.mbled.uni-stuttgart.de for an updated MBL database)1. MBLs in classes B1 and B3 are known for their ability to hydrolyse all β-lactam antibiotics, except monobactams, including penicillins, carbapenems and cephalosporins. The class B2 enzymes exhibit a narrower substrate preference and preferentially hydrolyse carbapenems2. The most clinically important MBLs belong to class B1, which contains VIM (Verona integrinencoded MBLs), IMP (imipenemase) and NDM (New Delhi MBL), and all of these enzymes have multiple clinical variants (VIM-1—VIM-46, IMP-1—IMP-51, and NDM-1—NDM-16) (www.lahey.org/Studies/). The presence of multiple variants poses a challenge to identify clinical inhibitors because the variants often exhibit different substrate specificities and are affected differently by known non-clinical inhibitors3.

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