Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:Q9UIJ5 (Rec)
 58,342 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The isoform specific role of sialic acid in human voltage-gated sodium channel gating was investigated through expression and chimeric analysis of two human isoforms, Na(v1.4) (hSkM1), and Na(v1.5) (hH1) in Chinese hamster ovary (CHO) cell lines. Immunoblot analyses indicate that both hSkM1 and hH1 are glycosylated and that hSkM1 is more glycosylated than hH1. Four sets of voltage-dependent parameters, the voltage of half-activation (V(a)), the voltage of half-inactivation (V(i)), the time constants for fast inactivation (tau(h)), and the time constants for recovery from inactivation (tau(rec)), were measured for hSkM1 and hH1 expressed in two CHO cell lines, Pro5 and Lec2, to determine the effect of changing sialylation on channel gating under conditions of full (Pro5) or reduced (Lec2) sialylation. For all parameters measured, hSkM1 gating showed a consistent 11-15 mV depolarizing shift under conditions of reduced sialylation, while hH1 showed no significant change in any gating parameter. Shifts in channel V(a) with changing external [Ca2+] indicated that sialylation of hSkM1, but not hH1, directly contributes to a negative surface potential. Functional analysis of two chimeras, hSkM1P1 and hH1P1, indicated that the responsible sialic acids are localized to the hSkM1 S5-S6 loop of domain I. When hSkM1 IS5-S6 was replaced by the analogous hH1 loop (hSkM1P1), changing sialylation had no significant effect on any voltage-dependent parameter. Conversely, when hSkM1 IS5-S6 was added to hH1 (hH1P1), all four parameters shifted by 6-7 mV in the depolarized direction under conditions of reduced sialylation. In summary, the gating of two human sodium channel isoforms show very different dependencies on sialic acid, with hSkM1 gating uniformly altered by sialic acid levels through an apparent electrostatic mechanism, while hH1 gating is unaffected by changing sialylation. Sialic acid-dependent gating can be removed or created by replacing or inserting hSkM1 IS5-S6, respectively, indicating that the functionally relevant sialic acid residues are localized to the first domain of the channel.
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PMID:Isoform-specific effects of sialic acid on voltage-dependent Na+ channel gating: functional sialic acids are localized to the S5-S6 loop of domain I. 1182 57

Morphological and histochemical analyses were performed to characterize the histology, ultrastructure, and glycosylation pattern of the jejunum and ileum of the wild rodent Lagostomus maximus. Enterocytes, goblet cells, Paneth cells, and enteroendocrine cells were identified in both intestinal epithelia. Two morphological types of enterocytes were identified only in the ileum based on their cytoplasm electron density. Although the histological and ultrastructural examination showed that the epithelia of both anatomical regions were morphologically similar, a certain specialization in their secretory products was evident. The glycosylation pattern of the jejunum and ileum was characterized in situ by histochemical and lectin histochemical methods. Histochemical results revealed the presence of carboxylated and sulfated gycoconjugates in both regions, although sulfomucins were clearly prevalent in the ileum. Sialic acid was highly O-acetylated and particularly abundant in the jejunum. The KOH/PA*/Bh/PAS technique evidenced a more intense histochemical reaction in the jejunal than in the ileum goblet cells, demonstrating a reduction of neutral mucin secretion in the distal small intestine. Further specific differences were revealed by lectin histochemistry. These data evidenced that the nature of mucus varies at different anatomical regions, probably adapted to physiological requirements.
Anat Rec (Hoboken) 2016 May
PMID:Comparative Analysis of the Morphology, Ultrastructure, and Glycosylation Pattern of the Jejunum and Ileum of the Wild Rodent Lagostomus maximus. 2691 39