BACKGROUND: Procollagen C-proteinase (PCP) enhancer 1 (PCPE1) specifically stimulates the PCP activity of bone morphogenic protein 1 (BMP1), a multisubstrate enzyme essential to the formation of extracellular matrix, via direct interaction with its substrate procollagen. Thus, in this study we sought to determine if serum PCPE1 (sPCPE1), a regulator of collagen formation, can be used as a diagnostic marker of collagen metabolism/remodeling. METHODS: We developed a method to track sPCPE1, and the findings were applied to evaluate the association of sPCPE1 glycopatterns with growth and presence of bone complication. RESULTS: Isoelectric focusing revealed that sPCPE1 has a multi-band appearance and that sPCPE1 glycopatterns are due to an N-linked oligosaccharide decorated with sialic acid. Evaluation of PCPE1 glycopatterns in different groups of subjects revealed a significant difference among preterm babies, term babies, and adults. Furthermore, in adults with breast cancer, the glycopattern intensity correlated with the presence of bone metastasis. CONCLUSIONS: The sPCPE1 glycopattern appears to be associated with the physiological and pathological states of bone. This study shows for the first time sPCPE1 glycopattern and suggest that changes in glycosylation of the protein may be in correlation with collagen metabolism. Studies are currently underway to determine its appearance in the serum of normal population on one hand and its appearance during growth and metabolic bone diseases on the other hand.
BACKGROUND:Procollagen C-proteinase (PCP) enhancer 1 (PCPE1) specifically stimulates the PCP activity of bone morphogenic protein 1 (BMP1), a multisubstrate enzyme essential to the formation of extracellular matrix, via direct interaction with its substrate procollagen. Thus, in this study we sought to determine if serum PCPE1 (sPCPE1), a regulator of collagen formation, can be used as a diagnostic marker of collagen metabolism/remodeling. METHODS: We developed a method to track sPCPE1, and the findings were applied to evaluate the association of sPCPE1 glycopatterns with growth and presence of bone complication. RESULTS: Isoelectric focusing revealed that sPCPE1 has a multi-band appearance and that sPCPE1 glycopatterns are due to an N-linked oligosaccharide decorated with sialic acid. Evaluation of PCPE1 glycopatterns in different groups of subjects revealed a significant difference among preterm babies, term babies, and adults. Furthermore, in adults with breast cancer, the glycopattern intensity correlated with the presence of bone metastasis. CONCLUSIONS: The sPCPE1 glycopattern appears to be associated with the physiological and pathological states of bone. This study shows for the first time sPCPE1 glycopattern and suggest that changes in glycosylation of the protein may be in correlation with collagen metabolism. Studies are currently underway to determine its appearance in the serum of normal population on one hand and its appearance during growth and metabolic bone diseases on the other hand.