PMID- 10534120
OWN - NLM
STAT- MEDLINE
DCOM- 19991118
LR  - 20210510
IS  - 0741-5400 (Print)
IS  - 0741-5400 (Linking)
VI  - 66
IP  - 4
DP  - 1999 Oct
TI  - Characterization of the biosynthesis, processing, and sorting of human
      HBP/CAP37/azurocidin.
PG  - 634-43
AB  - Azurocidin is a multifunctional endotoxin-binding serine protease homolog
      synthesized during the promyelocytic stage of neutrophil development. To
      characterize the biosynthesis and processing of azurocidin, cDNA encoding human
      preproazurocidin was stably transfected to the rat basophilic leukemia cell line 
      RBL-1 and the murine myeloblast-like cell line 32D cl3; cell lines previously
      utilized to study the related proteins cathepsin G and proteinase 3. After 30 min
      of pulse radiolabeling, two forms of newly synthesized proazurocidin (34.5 and 37
      kDa), differing in carbohydrate content but with protein cores of identical
      sizes, were recognized. With time, the 34.5-kDa form disappeared, while the
      37-kDa form was further processed proteolytically, as judged by digestion with
      N-glycosidase F. Conversion of high-mannose oligosaccharides into complex forms
      was shown by acquisition of complete resistance to endoglycosidase H.
      Radiosequence analysis demonstrated that the amino-terminal seven amino acid
      propeptide of proazurocidin was removed in a stepwise manner during processing;
      initial removal of five amino acids was followed by cleavage of a dipeptide.
      Presence of the protease inhibitors Gly-Phe-diazomethyl ketone, bestatin, or
      leupeptin inhibited only the cleavage of the dipeptide, thus indicating the
      involvement of at least two amino-terminal processing enzymes. Translocation of
      azurocidin to granules was shown by subcellular fractionation. Similar results,
      with efficient biosynthesis, processing, and targeting to granules in both cell
      lines, were obtained with a mutant form of human preproazurocidin lacking the
      amino-terminal heptapropeptide. In conclusion, this investigation is an important
      addition to our previous studies on related azurophil granule proteins, and
      provides novel information concerning the biosynthesis and distinctive
      amino-terminal processing of human azurocidin.
FAU - Lindmark, A
AU  - Lindmark A
AD  - Department of Hematology, Lund University, Sweden.
FAU - Garwicz, D
AU  - Garwicz D
FAU - Rasmussen, P B
AU  - Rasmussen PB
FAU - Flodgaard, H
AU  - Flodgaard H
FAU - Gullberg, U
AU  - Gullberg U
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Leukoc Biol
JT  - Journal of leukocyte biology
JID - 8405628
RN  - 0 (AZU1 protein, human)
RN  - 0 (Amino Acids)
RN  - 0 (Antimicrobial Cationic Peptides)
RN  - 0 (Blood Proteins)
RN  - 0 (Carrier Proteins)
RN  - 0 (Glycoproteins)
RN  - 0 (Monocyte Chemoattractant Proteins)
RN  - 0 (Protein Precursors)
RN  - 0 (Sulfur Radioisotopes)
RN  - 7006-34-0 (Asparagine)
SB  - IM
MH  - Amino Acids
MH  - Animals
MH  - Antimicrobial Cationic Peptides
MH  - Asparagine/metabolism
MH  - Biological Transport
MH  - Blood Proteins/biosynthesis/genetics/*metabolism
MH  - Carbohydrate Metabolism
MH  - Carrier Proteins/biosynthesis/genetics/*metabolism
MH  - Gene Expression
MH  - Glycoproteins/biosynthesis/genetics/*metabolism
MH  - Humans
MH  - Isotope Labeling
MH  - Mice
MH  - Monocyte Chemoattractant Proteins/biosynthesis/genetics/*metabolism
MH  - Protein Precursors/biosynthesis/genetics/*metabolism
MH  - *Protein Processing, Post-Translational
MH  - Rabbits
MH  - Rats
MH  - Sulfur Radioisotopes
MH  - Tumor Cells, Cultured
EDAT- 1999/10/26 00:00
MHDA- 1999/10/26 00:01
CRDT- 1999/10/26 00:00
PHST- 1999/10/26 00:00 [pubmed]
PHST- 1999/10/26 00:01 [medline]
PHST- 1999/10/26 00:00 [entrez]
AID - 10.1002/jlb.66.4.634 [doi]
PST - ppublish
SO  - J Leukoc Biol. 1999 Oct;66(4):634-43. doi: 10.1002/jlb.66.4.634.