The detection and identification of the Cr1-like membrane binding protein of porcine erythrocytes | [Journal of Animal and Plant sciences • 2024]

Author(s):

1. Z. Zeting: Shanxi Provincial Key Laboratory of Modernization of Chinese Veterinary Medicine, School of Animal Medicine, Shanxi Agricultural University, Taigu, 030801, Shanxi, China.

2. R. Qing: Shanxi Provincial Key Laboratory of Modernization of Chinese Veterinary Medicine, School of Animal Medicine, Shanxi Agricultural University, Taigu, 030801, Shanxi, China.

3. Z. Zheng: Shanxi Provincial Key Laboratory of Modernization of Chinese Veterinary Medicine, School of Animal Medicine, Shanxi Agricultural University, Taigu, 030801, Shanxi, China.

4. F. Kuohai: Shanxi Provincial Key Laboratory of Modernization of Chinese Veterinary Medicine, Laboratory Animal Management Centre, Shanxi Agricultural University, Taigu, 030801, Shanxi, China

5. S. Na: Shanxi Provincial Key Laboratory of Modernization of Chinese Veterinary Medicine, School of Animal Medicine, Shanxi Agricultural University, Taigu, 030801, Shanxi, China.

6. S. Panpan: Shanxi Provincial Key Laboratory of Modernization of Chinese Veterinary Medicine, School of Animal Medicine, Shanxi Agricultural University, Taigu, 030801, Shanxi, China.

7. L. Hongquan: Shanxi Provincial Key Laboratory of Modernization of Chinese Veterinary Medicine, School of Animal Medicine, Shanxi Agricultural University, Taigu, 030801, Shanxi, China.

8. Y. Wei: Shanxi Provincial Key Laboratory of Modernization of Chinese Veterinary Medicine, School of Animal Medicine, Shanxi Agricultural University, Taigu, 030801, Shanxi, China.

Abstract:

Erythrocyte complement receptor I-like (ECR1-like) is a natural immunoreactive molecule on the surface of porcine erythrocyte membrane. The aim of this study was to establish an effective method for the detection and characterization of porcine erythrocyte CR1-like membrane-bound proteins, and to explore their expression characteristics and biological significance in porcine erythrocyte membranes. The CR1-like protein ligands were observed by laser confocal microscopy using fluorescence immunocytochemistry with two types of PDZ-binding domain monoclonal antibodies, FAP-1 (Fas-associated phosphatase-1) and ZO2 (Tight Junction Protein ZO-2); meanwhile, immunoprecipitation and Western blot techniques were used to detect the membrane proteins of porcine blood cells. The immunofluorescence cytochemical staining showed that the specific fluorescence sites of CR1-like and FAP-1 molecules in the porcine erythrocyte membrane skeleton were identical; the sum of the difference squares of the site distances of 253 typical positive erythrocytes was 0.2224, indicating that the difference between the site distances of CR1-like and FAP-1 in each group was approximately 0. The results showed that the distribution of CR1-like and FAP-1 was consistent with a colocal relationship, and the FAP-1 molecule was clearly observed in the examined gel by immunoprecipitation. The results indicate that CR1-like does not bind directly to the erythrocyte membrane skeleton protein, but is distributed on the surface of the porcine erythrocyte membrane through the riveted structure of the FAP-1 protein molecule.

Page(s): 1331-1339

DOI: 10.36899/JAPS.2024.5.0814

Published: Journal: Journal of Animal and Plant sciences, Volume: 34, Issue: 5, Year: 2024

Keywords:

FAP1 , Immunoadhesion , CR1like , Porcine erythrocytes

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