L-asparaginase is an
enzyme that in humans is encoded by the ASRGL1gene.[5]
Function
The ASRGL1 protein consists of 308 amino acids and is activated by autocleavage at amino acid 168 to form an alpha- and a beta-chain, which can dimerize into a heterodimer.[6] The ASRGL1 enzyme has both L-asparaginase and beta-aspartyl peptidase activity and may be involved in the production of L-aspartate, which can act as an excitatory neurotransmitter in some brain regions.
According to antibody-based profiling and transcriptomics analysis, ASRGL1 protein is present in all analysed human tissues, with highest expression in brain, in female tissues such as the
uterine cervix and
fallopian tube, and in male tissues as
testis.[7] Based on
confocal microscopy ASRGL1 is mainly localized to the
microtubules.[8]
Clinical significance
ASRGL1 is highly expressed in the normal
endometrium and differentially expressed in
endometrial cancer. Loss of ASRGL1 expression is an unfavorable prognostic feature for patients with endometrial cancer.[9][10]
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56.
doi:
10.1016/S0378-1119(97)00411-3.
PMID9373149.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4.
doi:
10.1016/0378-1119(94)90802-8.
PMID8125298.
L-asparaginase is an
enzyme that in humans is encoded by the ASRGL1gene.[5]
Function
The ASRGL1 protein consists of 308 amino acids and is activated by autocleavage at amino acid 168 to form an alpha- and a beta-chain, which can dimerize into a heterodimer.[6] The ASRGL1 enzyme has both L-asparaginase and beta-aspartyl peptidase activity and may be involved in the production of L-aspartate, which can act as an excitatory neurotransmitter in some brain regions.
According to antibody-based profiling and transcriptomics analysis, ASRGL1 protein is present in all analysed human tissues, with highest expression in brain, in female tissues such as the
uterine cervix and
fallopian tube, and in male tissues as
testis.[7] Based on
confocal microscopy ASRGL1 is mainly localized to the
microtubules.[8]
Clinical significance
ASRGL1 is highly expressed in the normal
endometrium and differentially expressed in
endometrial cancer. Loss of ASRGL1 expression is an unfavorable prognostic feature for patients with endometrial cancer.[9][10]
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56.
doi:
10.1016/S0378-1119(97)00411-3.
PMID9373149.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4.
doi:
10.1016/0378-1119(94)90802-8.
PMID8125298.