Publications by authors named "N Kartner"
Article Synopsis
- The subunit is a key component of the V-ATPase complex, with four isoforms in mammals that help target V-ATPases to specific locations within cells.
- Research on mutations in these isoforms, particularly regarding human diseases like cutis laxa and dRTA, aims to identify crucial parts needed for V-ATPase function.
- Experimental findings show that certain mutations lead to instability and improper trafficking of the subunits, providing insights for potential drug design to treat these conditions.
The a subunit of the V membrane-integrated sector of human V-ATPase has four isoforms, a1-a4, with diverse and crucial functions in health and disease. They are encoded by four conserved paralogous genes, and their vertebrate orthologs have positionally conserved N-glycosylation sequons within the second extracellular loop, EL2, of the a subunit membrane domain. Previously, we have shown directly that the predicted sequon for the a4 isoform is indeed N-glycosylated.
View Article and Find Full Text PDFRecombinant human bone morphogenetic protein 2 (rhBMP-2) is used clinically to enhance implant-mediated bone regeneration. However, there are risks associated with the high rhBMP-2 dose that is required in the implant to mitigate diffusional loss over the therapeutic timespan. On-demand, localized control over delivery of rhBMP-2, days after implantation, would therefore be an attractive solution in the area of bone repair and reconstruction, yet this has posed a significant challenge, with little data to support in vivo efficacy to date.
View Article and Find Full Text PDFArticle Synopsis
- The a subunit is part of the V-ATPase complex with four isoforms in mammals, implicated in various diseases, but its structure and function are not fully understood.
- This study specifically investigates whether the human a4 isoform is N-glycosylated at the predicted site Asn489, using HEK 293 cells to express the a4 subunit with and without mutations.
- Results show that N-glycosylation enhances a4 stability and is essential for its proper trafficking to the plasma membrane, while unglycosylated a4 is retained in the endoplasmic reticulum and degrades faster.
Introduction: Bone loss occurs in many diseases, including osteoporosis, rheumatoid arthritis and periodontal disease. For osteoporosis alone, it is estimated that 75 million people are afflicted worldwide, with high risks of fractures and increased morbidity and mortality. The demand for treatment consumes an ever-increasing share of healthcare resources.
View Article and Find Full Text PDF