Asprich: A Novel Aspartic Acid-Rich Protein Family from the Prismatic Shell Matrix of the Bivalve Atrina rigida

ChemBioChem ◽  
2005 ◽  
Vol 6 (2) ◽  
pp. 304-314 ◽  
Author(s):  
Bat-Ami Gotliv ◽  
Naama Kessler ◽  
Jan L. Sumerel ◽  
Daniel E. Morse ◽  
Noreen Tuross ◽  
...  
Keyword(s):  
Aspartic Acid ◽  
Protein Family ◽  
Shell Matrix ◽  
Prismatic Shell ◽  
Atrina Rigida

The Effect of Exogenous Fluoride on the Calcium PUMP, Ciliary Activity, and Shell Formation of the Fingernail Clam, Musculium Transversum

1982 ◽  
Vol 40 ◽  
pp. 58-59
Author(s):  
Anthony Paparo ◽  
Judy A. Murphy ◽  
Robert Dean
Keyword(s):  
Mississippi River ◽  
Calcium Pump ◽  
Bottom Fauna ◽  
Ciliary Activity ◽  
Shell Formation ◽  
Middle Reach ◽  
Shell Matrix ◽  
Fingernail Clams ◽  
Ca Carbonate

In the mid-1950's, fingernail clams virtually disappeared from a 100-mile section of the IL River, a tributary of the Mississippi River, due to unknown causes. A survey of the bottom fauna of the IL River in 1979, revealed that the clams were still absent from the middle reach of the River, where they had been abundant prior to the die-off in the 1950's. Some factor(s) in the River currently prevent the clams from recolonizing areas where they were formerly abundant. Recently, clams exposed to fluoride developed abnormal grooves in the shell matrix. Fluorides are known to be protoplasmic poisons removing essential body calcium by precipitation. Since the shell consists primarily of Ca carbonate, this investigation examines the possible role of fluoride on shell formation and the poisoning of the Ca pump which can directly inhibit lateral ciliary activity on the gill.

Investigating the functional link between TMEM165 and SPCA1

2019 ◽  
Vol 476 (21) ◽  
pp. 3281-3293 ◽  
Author(s):  
Elodie Lebredonchel ◽  
Marine Houdou ◽  
Hans-Heinrich Hoffmann ◽  
Kateryna Kondratska ◽  
Marie-Ange Krzewinski ◽  
...  
Keyword(s):  
Subcellular Localization ◽  
Complete Loss ◽  
Protein Family ◽  
Uncharacterized Protein ◽  
Functional Link ◽  
P Type

TMEM165 was highlighted in 2012 as the first member of the Uncharacterized Protein Family 0016 (UPF0016) related to human glycosylation diseases. Defects in TMEM165 are associated with strong Golgi glycosylation abnormalities. Our previous work has shown that TMEM165 rapidly degrades with supraphysiological manganese supplementation. In this paper, we establish a functional link between TMEM165 and SPCA1, the Golgi Ca2+/Mn2+ P-type ATPase pump. A nearly complete loss of TMEM165 was observed in SPCA1-deficient Hap1 cells. We demonstrate that TMEM165 was constitutively degraded in lysosomes in the absence of SPCA1. Complementation studies showed that TMEM165 abundance was directly dependent on SPCA1's function and more specifically its capacity to pump Mn2+ from the cytosol into the Golgi lumen. Among SPCA1 mutants that differentially impair Mn2+ and Ca2+ transport, only the Q747A mutant that favors Mn2+ pumping rescues the abundance and Golgi subcellular localization of TMEM165. Interestingly, the overexpression of SERCA2b also rescues the expression of TMEM165. Finally, this paper highlights that TMEM165 expression is linked to the function of SPCA1.

The involvement of the GGA protein family in BACE transport and APP processing in Alzheimer's disease

2008 ◽  
Vol 35 (S 01) ◽  
Author(s):  
C Steinmetz ◽  
B von Einem ◽  
D Schwanzar ◽  
F Dolp ◽  
A.C Ludolph ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Protein Family ◽  
App Processing

Analysis of Aspartic Acid at Position 9 of the HLA-C Molecule in Patients with Psoriasis Vulgaris.

1996 ◽  
Vol 58 (6) ◽  
pp. 991-993
Author(s):  
Eishin MORITA ◽  
Susumu SHINODA ◽  
Eiichi GYOTOKU ◽  
Satoko HIHARA ◽  
Shoso YAMAMOTO
Keyword(s):  
Aspartic Acid ◽  
Psoriasis Vulgaris
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