Identification of the motifs and amino acids in aggrecan G1 and G2 domains involved in product secretion
| Autor: | Yaojiong Wu, Burton B. Yang, Jianping Wen, Wang Sheng, Liwen Chen, Liu Cao, Chris Kiani, Peng-Sheng Zheng, Mark E. Adams, Vivian Lee |
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| Rok vydání: | 2003 |
| Předmět: |
Repetitive Sequences
Amino Acid Amino Acid Motifs Restriction Mapping Endoplasmic Reticulum Transfection Biochemistry Mice Tandem repeat Two-Hybrid System Techniques Yeasts Animals Humans Secretion Lectins C-Type Aggrecans Aggrecan Calcium metabolism chemistry.chemical_classification Extracellular Matrix Proteins biology Base Sequence Sequence Homology Amino Acid Endoplasmic reticulum Membrane Proteins Yeast Recombinant Proteins Amino acid Protein Structure Tertiary Rats chemistry Chondroitin Sulfate Proteoglycans Mutagenesis COS Cells biology.protein Cattle Proteoglycans Antibody Chickens |
| Zdroj: | Biochemistry. 42(23) |
| ISSN: | 0006-2960 |
| Popis: | Members of the large aggregating chondroitin sulfate proteoglycans are characterized by an N-terminal fragment known as Gl domain, which is composed of an immunoglobulin (IgG)-like motif and two tandem repeats (TR). Previous studies have indicated that the expressed product of aggrecan G1 domain was not secreted. Here we demonstrated that the inability of G 1 secretion was associated with the tandem repeats but not the IgG-like motif, and specifically with TR1 of aggrecan. We also demonstrated that the G2 domain, a domain unique to aggrecan, had a similar effect on product secretion. The sequence of TRI of Gl is highly conserved across species, which suggested similar functions played by these motifs. In a yeast two-hybrid assay, TR 1 interacted with the calcium homeostasis endoplasmic reticulum protein. Deletion/mutation experiments indicated that the N-terminal fragment of TR1, in particular, the amino acids H 2 R 4 of this motif were key to its effect on product secretion. However, the N-terminal 55 amino acids were required to exert this function. Taken together, our study suggests a possible molecular mechanism for the function of the tandem repeats in product processing. |
| Databáze: | OpenAIRE |
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