Arsenic-Induced Congenital Malformations in Genetically Susceptible Folate Binding Protein-2 Knockout Mice

2001 ◽  
Vol 177 (3) ◽  
pp. 238-246 ◽  
Author(s):  
Bogdan Wlodarczyk ◽  
Ofer Spiegelstein ◽  
Janée Gelineau-van Waes ◽  
Roseann L. Vorce ◽  
Xiufen Lu ◽  
...  
2003 ◽  
Vol 67 (12) ◽  
pp. 974-978 ◽  
Author(s):  
Ofer Spiegelstein ◽  
Michelle Y. Merriweather ◽  
Ned J. Wicker ◽  
Richard H. Finnell

2004 ◽  
Vol 231 (1) ◽  
pp. 221-231 ◽  
Author(s):  
Ofer Spiegelstein ◽  
Laura E. Mitchell ◽  
Michelle Y. Merriweather ◽  
Ned J. Wicker ◽  
Qiang Zhang ◽  
...  

Reproduction ◽  
2017 ◽  
Vol 154 (6) ◽  
pp. 723-733 ◽  
Author(s):  
Huijuan Zhang ◽  
Guishuan Wang ◽  
Lin Liu ◽  
Xiaolin Liang ◽  
Yu Lin ◽  
...  

The chromatoid body (CB) is a specific cloud-like structure in the cytoplasm of haploid spermatids. Recent findings indicate that CB is identified as a male germ cell-specific RNA storage and processing center, but its function has remained elusive for decades. In somatic cells, KH-type splicing regulatory protein (KSRP) is involved in regulating gene expression and maturation of select microRNAs (miRNAs). However, the function of KSRP in spermatogenesis remains unclear. In this study, we showed that KSRP partly localizes in CB, as a component of CB. KSRP interacts with proteins (mouse VASA homolog (MVH), polyadenylate-binding protein 1 (PABP1) and polyadenylate-binding protein 2 (PABP2)), mRNAs (Tnp2 and Odf1) and microRNAs (microRNA-182) in mouse CB. Moreover, KSRP may regulate the integrity of CB via DDX5-miRNA-182 pathway. In addition, we found abnormal expressions of CB component in testes of Ksrp-knockout mice and of patients with hypospermatogenesis. Thus, our results provide mechanistic insight into the role of KSRP in spermatogenesis.


2017 ◽  
Vol 142 (3) ◽  
pp. 420-428 ◽  
Author(s):  
Nico Mitro ◽  
Gaia Cermenati ◽  
Matteo Audano ◽  
Silvia Giatti ◽  
Marzia Pesaresi ◽  
...  

1987 ◽  
Vol 252 (4) ◽  
pp. F757-F760 ◽  
Author(s):  
J. Selhub ◽  
S. Nakamura ◽  
F. A. Carone

Surface proximal convoluted tubules (PCT) in rats were microinfused in situ with [3H]folic acid to study the role of folate binding protein (FBP) in the kidney brush-border membrane for renal conservation and transport of folate [3H]folic acid absorption was linearly related to tubular length of PCT and occurred largely in this segment of the tubule. Unlabeled folate derivatives inhibited [3H]folic acid absorption, the extent of which was dependent on the type of unlabeled folate used and its concentration. At equivalent concentrations, inhibition was most effective with unlabeled folic acid, slightly lower than with 5-methyltetrahydrofolate and least effective with methotrexate. Comparisons between [3H]folic acid absorption before and after infusion of a saturating dose of unlabeled folic acid or repetitive injections of [3H]folic acid into the same tubular site revealed continuous and rapid regeneration of unsaturated folic acid uptake sites with an apparent half-life of 28.75 +/- 8.75 s. Determination of [3H] retained in the tubule at various periods after microinfusion of [3H]folic acid revealed slow cellular disappearance with an apparent half-life of 47.3 +/- 5.4 min. It is proposed that the brush-border FBP functions as a receptor of infused folic acid and that following the binding of the ligand the folic acid/FBP complex undergoes a rapid change that results in the internalization of folic acid and regeneration of unsaturated binding sites at the membrane surface. Internalized folic acid is slowly released into renal capillaries.


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