Amino acid composition and immunochemical properties of AcPase III and AcPase IV representing glycoforms of the lower molecular weight, tartrate-resistant acid phosphatase of the frog liver

Szalewicz, Agata; Jańska, Hanna; Strzelczyk, Barbara; Kubicz, Aleksandra

doi:10.1016/0020-711x(92)90106-b

Cited by 5 publications

(5 citation statements)

References 14 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Cotranslational and posttranslational glycan alterations appear to be of fundamental biological importance because they provide a mechanism to fine‐tune glycoprotein function within the cell. Changes in glycan composition and structure can therefore lead to glycosylated variants of the same protein referred to as “glycoform.” Glycoforms frequently differ in their activity and/or ligand‐binding specificity and have been well established for a broad range of animal glycoproteins including ribonucleases, proteases, APases, and immunoglobulins (Maeda & Kimura, ; Navazio et al, ; Rudd et al, ; Szalewicz, Jańska, Strzelczyk, & Kubicz, ). Although plant glycoforms appear to be equally prevalent (Xu, Medzihradszky, Wang, Burlingame & Chalkley, ), there are few comprehensive studies of plant glycoforms.…”

Section: Discussionmentioning

confidence: 99%

“…Changes in glycan composition and structure can therefore lead to glycosylated variants of the same protein referred to as "glycoform." Glycoforms frequently differ in their activity and/or ligand-binding specificity and have been well established for a broad range of animal glycoproteins including ribonucleases, proteases, APases, and immunoglobulins (Maeda & Kimura, 2006;Navazio et al, 2002;Rudd et al, 1995;Szalewicz, Jańska, Strzelczyk, & Kubicz, 1992).…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

A glycoform of the secreted purple acid phosphatase AtPAP26 co‐purifies with a mannose‐binding lectin (AtGAL1) upregulated by phosphate‐starved Arabidopsis

Ghahremani

Tran

Biglou

et al. 2019

Plant Cell & Environment

View full text Add to dashboard Cite

The purple acid phosphatase AtPAP26 plays a central role in Pi-scavenging by Pi-starved (-Pi) Arabidopsis. Mass spectrometry (MS) of AtPAP26-S1 and AtPAP26-S2 glycoforms secreted by -Pi suspension cells demonstrated that N-glycans at Asn and Asn were modified in AtPAP26-S2 to form high-mannose glycans. A 55 kDa protein that co-purified with AtPAP26-S2 was identified as a Galanthus nivalis agglutinin-related and apple domain lectin-1 (AtGAL1; At1g78850). MS revealed that AtGAL1 was bisphosphorylated at Tyr and Thr , and glycosylated at four conserved Asn residues. When AtGAL was incubated in the presence of a thiol-reducing reagent prior to immunoblotting, its cross-reactivity with anti-AtGAL1-IgG was markedly attenuated (consistent with three predicted disulfide bonds in AtGAL1's apple domain). Secreted AtGAL1 polypeptides were upregulated to a far greater extent than AtGAL1 transcripts during Pi deprivation, indicating post-transcriptional control of AtGAL1 expression. Growth of a -Pi atgal1 mutant was unaffected, possibly due to compensation by AtGAL1's closest paralog, AtGAL2 (At1g78860). Nevertheless, AtGAL1's induction by numerous stresses combined with the broad distribution of AtGAL1-like lectins in diverse species implies an important function for AtGAL1 orthologs within the plant kingdom. We hypothesize that binding of AtPAP26-S2's high-mannose glycans by AtGAL1 enhances AtPAP26 function to facilitate Pi-scavenging by -Pi Arabidopsis.

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

A glycoform of the secreted purple acid phosphatase AtPAP26 co‐purifies with a mannose‐binding lectin (AtGAL1) upregulated by phosphate‐starved Arabidopsis

Ghahremani

Tran

Biglou

et al. 2019

Plant Cell & Environment

View full text Add to dashboard Cite

show abstract

“…Alkaline and acid phosphatase activities were calculated on the basis of the rate p-nitrophenol release from 2.5 mM nitrophenyl phosphate at pH 5 or pH 8.6, respectively, according to Szalewicz et al (1992). The hydrolysis of one μM of the substrate per minute was considered as the activity unit.…”

Section: Methodsmentioning

confidence: 99%

“…Cell cultures were incubated at 37OC for 72 h. The culture medium was discarded, the cells were rinsed in phosphate-buffered saline (PBS), and 1 mL of 0.025% solution of trypsin in PBS was added. The cells suspended in trypsin solution were counted under the microscope in a hemocytometer and cell viability was determined by standard trypan blue exclusion test (Szalewicz et al 1992). The protein level in the cells was determined with the Lowry et al (1951) method after washing the cells in PBS.…”

Section: Treatment Of Tumor Cellsmentioning

confidence: 99%

The Influence of Very Low Doses of Cisplatin on Tumor Cell ProliferationIn Vitroand on Some Hematological and Enzymatic Parameters of Healthy Rats

Malarczyk¹,

Kandefer‐Szerszeń

Jarosz-WilkoLazka³

2003

Nonlinearity in Biology, Toxicology, Medicine

View full text Add to dashboard Cite

Healthy rats had been treated for 2 or 6 weeks with 1.0 mL of and 10-l6 mg/ mL of cisplatin. After 2 weeks of treatment, a significant increase in leukocyte and erythrocyte count and also in hematocrit was observed. Among leukocytes the number of neutrophils and eosinophils significantly increased. Biochemical analyses indicated a decrease in the glycogen content in the liver and kidneys after 2 weeks of treatment with low doses of cisplatin but at the end of the experiment (8th week of experiment) the stores of glycogen increased significantly. Biochemical analyses concerning the activity of some enzymes in the liver revealed a significant increase of peroxidase and acid phosphatase as well as catalase activities after 2 weeks of treatment. However, catalase was induced by a very low concentration of cisplatin, 10-l6 mg/mL. After the cessation of cisplatin treatment the activity of enzymes returned to normal values.Human lung carcinoma cell line A,,, (ECACC No 86012804) was also studied after treatment with the same doses of cisplatin and inhibition of its growth was observed. The results of these experiments strongly indicated that low doses of cisplatin could be stimulating for healthy cells but cytostatic for tumor cells. Possible mechanisms involved in the biological activity of very low cisplatin concentrations are discussed.

show abstract

“…Paraffin sections were cut, dewaxed, hydrated through graded alcohol to PBS (pH 7.4) and treated with 1% hydrogen peroxide in methanol to abolish endogenous peroxidase activity. The sections were then probed with primary antibodies, i.e., polyclonal rabbit IgG directed against the LMW AcPase, prepared as described earlier (Szalewicz et al, 1992). In parallel experiments two kinds of antibodies, raised against the separated main forms of the enzyme differing in pI , i.e.…”

Section: Immunohistochemical Localization Of the Lmw Acpase In Frog Lmentioning

confidence: 99%

The 35 kDa acid metallophosphatase of the frog Rana esculenta liver: studies on its cellular localization and protein phosphatase activity.

Szalewicz¹,

Strzelczyk²,

Sopel³

et al. 2003

Acta Biochim Pol

Self Cite

View full text Add to dashboard Cite

The cellular localization of the 35 kDa, low molecular mass acid metallophosphatase (LMW AcPase) from the frog (Rana esculenta) liver and its activity towards P-Ser and P-Tyr phosphorylated peptides were studied. This enzyme was localized to the cytoplasm of hepatocytes but did not appear in other cells of liver tissue (endothelium, macrophages, blood cells). This LMW AcPase does not display activity towards (32)P-phosphorylase a under conditions standard for the enzymes of PPP family. Proteins containing P-Ser: rabbit (32)P-phosphorylasea and phosvitin are hydrolysed only at acidic pH and are poor substrates for this enzyme. The frog AcPase is not inhibited by okadaic acid and F(-) ions, the Ser/Thr protein phosphatase inhibitors. Moreover, the frog enzyme does not cross-react with specific antisera directed against N-terminal fragment of human PP2A and C-terminal conserved fragment of the eukaryotic PP2A catalytic subunits. These results exclude LMW AcPase from belonging to Ser/Thr protein phosphatases: PP1c or PP2Ac. In addition to P-Tyr, this enzyme hydrolyses efficiently at acidic pH P-Tyr phosphorylated peptides (hirudin and gastrin fragments). K(m) value for the hirudin fragment (7.55 +/- 1.59 x 10(-6) M) is 2-3 orders of magnitude lower in comparison with other substrates tested. The enzyme is inhibited competitively by typical inhibitors of protein tyrosine phosphatases (PTPases): sodium orthovanadate, molybdate and tungstate. These results may suggest that the LMW AcPase of frog liver can act as PTPase in vivo. A different cellular localization and different response to inhibition by tetrahedral oxyanions (molybdate, vanadate and tungstate) provide further evidence that LMW AcPase of frog liver is distinct from the mammalian tartrate-resistant acid phosphatases.

show abstract

Amino acid composition and immunochemical properties of AcPase III and AcPase IV representing glycoforms of the lower molecular weight, tartrate-resistant acid phosphatase of the frog liver

Cited by 5 publications

References 14 publications

A glycoform of the secreted purple acid phosphatase AtPAP26 co‐purifies with a mannose‐binding lectin (AtGAL1) upregulated by phosphate‐starved Arabidopsis

A glycoform of the secreted purple acid phosphatase AtPAP26 co‐purifies with a mannose‐binding lectin (AtGAL1) upregulated by phosphate‐starved Arabidopsis

The Influence of Very Low Doses of Cisplatin on Tumor Cell ProliferationIn Vitroand on Some Hematological and Enzymatic Parameters of Healthy Rats

The 35 kDa acid metallophosphatase of the frog Rana esculenta liver: studies on its cellular localization and protein phosphatase activity.

Contact Info

Product

Resources

About