WordNet

a thin pliable sheet of material
a pliable sheet of tissue that covers or lines or connects the organs or cells of animals or plants (同)tissue layer
insert (days) in a calendar

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(生物の)膜,皮膜
…‘を'間に入れる,挿入する / 〈うるうの日・月〉‘を'暦に入れる

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1. 代謝性アルカローシスの病因 pathogenesis of metabolic alkalosis
2. 血液-血液透析膜の相互作用に関与する生化学的機序 biochemical mechanisms involved in blood hemodialysis membrane interactions
3. 赤血球細胞膜の動態および機構 red blood cell membrane dynamics and organization
4. ライソゾーム膜蛋白質2欠損症（糖原病IIb型、ダノン病） lysosome associated membrane protein 2 deficiency glycogen storage disease iib danon disease
5. 血液透析膜の生体適合性についての臨床結果 clinical consequences of hemodialysis membrane biocompatibility

English Journal

Role of adaptor proteins and clathrin in the trafficking of human kidney anion exchanger 1 (kAE1) to the cell surface.

Junking M1, Sawasdee N, Duangtum N, Cheunsuchon B, Limjindaporn T, Yenchitsomanus PT.Author information 1Division of Molecular Medicine, Department of Research and Development, Faculty of Medicine Siriraj Hospital, Mahidol University, Bangkok, Thailand.AbstractKidney anion exchanger 1 (kAE1) plays an important role in acid-base homeostasis by mediating chloride/bicarbornate (Cl- /HCO3 - ) exchange at basolateral membrane of α-intercalated cells in distal nephron. Impaired intracellular trafficking of kAE1 caused by mutations of SLC4A1 encoding kAE1 results in kidney disease - distal renal tubular acidosis (dRTA). However, it is not known how the intracellular sorting and trafficking of kAE1 from trans-Golgi network (TGN) to the basolateral membrane occur. Here, we studied the role of basolateral-related sorting proteins, including mu1 subunit of adaptor protein (AP) complexes, clathrin, and protein kinase D, on kAE1 trafficking in polarized and non-polarized kidney cells. By using RNA interference, co-immunoprecipitation, yellow fluorescent protein-based protein fragment complementation assay, and immunofluorescence staining, we demonstrated that AP-1 mu1A, AP-3 mu1, AP-4 mu1 and clathrin (but not AP-1 mu1B, PKD1 or PKD2) play crucial roles in intracellular sorting and trafficking of kAE1. We also demonstrated co-localization of kAE1 and basolateral-related sorting proteins in human kidney tissues by double immunofluorescence staining. These findings indicate that AP-1 mu1A, AP-3 mu1, AP-4 mu1, and clathrin are required for kAE1 sorting and trafficking from TGN to the basolateral membrane of acid-secreting α-intercalated cells.
Traffic (Copenhagen, Denmark).Traffic.2014 Apr 3. doi: 10.1111/tra.12172. [Epub ahead of print]
Kidney anion exchanger 1 (kAE1) plays an important role in acid-base homeostasis by mediating chloride/bicarbornate (Cl- /HCO3 - ) exchange at basolateral membrane of α-intercalated cells in distal nephron. Impaired intracellular trafficking of kAE1 caused by mutations of SLC4A1 encoding kAE1 resul
PMID 24698155

βIV-Spectrin regulates TREK-1 membrane targeting in the heart.

Hund TJ1, Snyder JS, Wu X, Glynn P, Koval OM, Onal B, Leymaster ND, Unudurthi SD, Curran J, Camardo C, Wright PJ, Binkley PF, Anderson ME, Mohler PJ.Author information 1The Dorothy M. Davis Heart and Lung Research Institute, The Ohio State University Wexner Medical Center, 473 W. 12th Avenue, 43210 Columbus, OH, USA.AbstractAIMS: Cardiac function depends on the highly regulated and co-ordinate activity of a large ensemble of potassium channels that control myocyte repolarization. While voltage-gated K(+) channels have been well characterized in the heart, much less is known about regulation and/or targeting of two-pore K(+) channel (K2P) family members, despite their potential importance in modulation of heart function.
Cardiovascular research.Cardiovasc Res.2014 Apr 1;102(1):166-75. doi: 10.1093/cvr/cvu008. Epub 2014 Jan 20.
AIMS: Cardiac function depends on the highly regulated and co-ordinate activity of a large ensemble of potassium channels that control myocyte repolarization. While voltage-gated K(+) channels have been well characterized in the heart, much less is known about regulation and/or targeting of two-pore
PMID 24445605

Ammonia Transport in the Kidney by Rhesus Glycoproteins.

Weiner ID1, Verlander JW.Author information 11University of Florida College of Medicine.AbstractRenal ammonia metabolism is a fundamental element of acid-base homeostasis, comprising a major component of both basal and physiologically-altered renal net acid excretion. Over the past several years, a fundamental change in our understanding of the mechanisms of renal epithelial cell ammonia transport has occurred, replacing the previous model which was based upon diffusion equilibrium for NH3 and trapping of NH4+ with a new model in which specific and regulated transport of both NH3 and NH4+ across renal epithelial cell membranes via specific membrane proteins is required for normal ammonia metabolism. A major advance has been the recognition that members of a recently recognized transporter family, the Rhesus glycoprotein family, mediate critical roles in renal and extrarenal ammonia transport. The erythroid-specific Rhesus glycoprotein, Rh A Glycoprotein (Rhag), was the first member of this family recognized as an ammonia-specific transporter. Subsequently, the nonerythroid Rh glycoproteins, Rh B Glycoprotein (Rhbg) and Rh C Glycoprotein (Rhcg), were cloned and identified as ammonia transporters. They are expressed in specific cell populations and membrane domains in distal renal epithelial cells, where they facilitate ammonia secretion. In this review, we discuss the distribution of Rhbg and Rhcg in the kidney, the regulation of their expression and activity in physiologic disturbances, the effects of genetic deletion on renal ammonia metabolism, and the molecular mechanisms of Rh glycoprotein-mediated ammonia transport.
American journal of physiology. Renal physiology.Am J Physiol Renal Physiol.2014 Mar 19. [Epub ahead of print]
Renal ammonia metabolism is a fundamental element of acid-base homeostasis, comprising a major component of both basal and physiologically-altered renal net acid excretion. Over the past several years, a fundamental change in our understanding of the mechanisms of renal epithelial cell ammonia trans
PMID 24647713