TY - JOUR
T1 - PGRMC proteins are coming of age
T2 - A special issue on the role of PGRMC1 and PGRMC2 in metabolism and cancer biology
AU - Cahill, Michael A.
AU - Neubauer, Hans
PY - 2021/1/29
Y1 - 2021/1/29
N2 - This is a preface by the guest editors of the special issue of Cancers featuring the biology of progesterone (P4) receptor membrane component (PGRMC) proteins as it relates to metabolism and cancer. PGRMC proteins are members of the cytochrome b5-related membrane-associated progesterone receptor (MAPR) family, of which humans have four members: PGRMC1, PGRMC2, Neudes in and Neuferricin [1,2]. In the early 2000s, we were both part of a German Human Genome Project (Proteomanalyse von Brustkrebsgenen, 01 KW0102, 2001–2004) that focused on the development of highly sensitivity proteomics methods for the identification of proteins whose properties were altered between clinical protein samples. Before the rise and supremacy of mass spectrometric proteomics methods, we developed an advanced gel electrophoresis and highly sensitive/accurate differential detection method to examine cryoconserved breast cancer tissues, comparing estrogen receptor positive versus negative patient cohorts [3,4].Of the many hundreds of proteins identified (and manually biologically assessed in those days), we detected three differently charged isoforms of PGRMC1 [4].
AB - This is a preface by the guest editors of the special issue of Cancers featuring the biology of progesterone (P4) receptor membrane component (PGRMC) proteins as it relates to metabolism and cancer. PGRMC proteins are members of the cytochrome b5-related membrane-associated progesterone receptor (MAPR) family, of which humans have four members: PGRMC1, PGRMC2, Neudes in and Neuferricin [1,2]. In the early 2000s, we were both part of a German Human Genome Project (Proteomanalyse von Brustkrebsgenen, 01 KW0102, 2001–2004) that focused on the development of highly sensitivity proteomics methods for the identification of proteins whose properties were altered between clinical protein samples. Before the rise and supremacy of mass spectrometric proteomics methods, we developed an advanced gel electrophoresis and highly sensitive/accurate differential detection method to examine cryoconserved breast cancer tissues, comparing estrogen receptor positive versus negative patient cohorts [3,4].Of the many hundreds of proteins identified (and manually biologically assessed in those days), we detected three differently charged isoforms of PGRMC1 [4].
U2 - 10.3390/cancers13030512
DO - 10.3390/cancers13030512
M3 - Editorial
C2 - 33572771
VL - 13
SP - 1
EP - 8
JO - Cancers
JF - Cancers
SN - 2072-6694
IS - 3
M1 - 512
ER -
