Ultrastructural, histochemical and immunohistochemical features of porcine intestinal lamina propria macrophages (LPMs), peripheral blood fibronectin-adherent cells (FACs) and splenic-adherent cells (SPACs) were compared. Freshly isolated FACs and SPACs were small and showed small cytoplasmic processes, little evidence of endocytic vacuoles, few lysosomes and sparse rough endoplasmic reticulum (RER). Fresh FACs were negative for acid phosphatase, non-specific esterase (NSE) and beta-galactosidase activity. Of the SPACs, 20-40% were positive for acid phosphatase, < 5% for NSE and 5-10% for beta-galactosidase. Pre-cultured FACs and SPACs were large and showed an abundance of endocytic vacuoles; they possessed dilated and prominent RER and > 95% were positive for the three enzyme activities. LPMs exhibited abundant endocytic vacuoles or vesicles and lysosomes but sparse RER, and > 85% were positive for the three enzymes. LPMs (24%), FACs (49%) and SPACs (40%) expressed MHC (major histocompatibility complex) class II glycoproteins. Macrophage-granulocyte antigens were detected in LPMs (14%), FACs (50%) and SPACs (33%). The results thus suggest that freshly isolated FACs differ from LPMs morphologically and in enzymic features, and the differences may represent part of the cell maturation process.
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http://dx.doi.org/10.1016/s0021-9975(05)80090-8 | DOI Listing |
Front Plant Sci
December 2024
College of Life Sciences, Fujian Agriculture and Forestry University, Fujian, China.
The mitochondrial pyruvate dehydrogenase complex (PDC) plays a crucial role in linking the glycolysis pathway and the tricarboxylic acid (TCA) cycle. Previously, we reported that a mutation of , encoding an E1β subunit of PDC, affects the abundance of auxin efflux carriers PIN-FORMED proteins (PINs) via reduced recycling and enhanced degradation in vacuoles. Here, we further analyzed the effects of TCA cycle inhibition on vesicle trafficking using both the mutant and 3-BP, a TCA cycle inhibitor.
View Article and Find Full Text PDFLife Sci Alliance
February 2025
Division of Life Science, The Hong Kong University of Science and Technology, Kowloon, SAR of China
The plasma membrane has a complex organization that includes the polarized distribution of membrane proteins and lipids. Glycosylphosphatidylinositol-anchored proteins (GPI-APs) are ubiquitously expressed in eukaryotes and represent a functionally diverse, extensively remodeled, ER-derived group of proteins critical for the organization and function of the plasma membrane. Little is known about how the transport of incompletely remodeled GPI-APs to the plasma membrane affects cell function.
View Article and Find Full Text PDFPLoS Pathog
November 2024
Department of Microbiology and Infection Control, University Hospital of North Norway, Tromsø, Norway.
BK polyomavirus (BKPyV) is a ubiquitous human virus that establishes a persistent infection in renal tubular epithelial cells and mainly causes disease in kidney transplant recipients. The closely related simian polyomavirus SV40 is known to cause cytoplasmic vacuolization in simian kidney cells, possibly increasing progeny release and cell death. This study aimed to determine whether BKPyV causes cytoplasmic vacuolization in primary human renal proximal tubule epithelial cells (RPTECs) and to investigate its potential role in the replication cycle.
View Article and Find Full Text PDFVirulence
December 2024
Xinxiang Key Laboratory of Pathogenic Biology, Department of Pathogenic Biology, School of Basic Medical Sciences, Xinxiang Medical University, Xinxiang, Henan, PR China.
Prenyltransferases act essential roles in the prenylation modification, which is significant for proteins, like small GTPases to execute various important activities in (). The structures and partial functions of prenyltransferases (FTase, GGTase-I, and GGTase-II) in prenylation process have been dissected in . However, the cellular effects of prenyltransferases on type 2-ME49 strain of are largely unknown.
View Article and Find Full Text PDFInt J Biol Macromol
December 2024
Department of Food Biotechnology, Instituto de Agroquímica y Tecnología de Alimentos (IATA), Consejo Superior de Investigaciones Científicas (CSIC), Paterna, Spain.. Electronic address:
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