Judith S. Bond
Photo
Academic title Professor and Chair Biochemistry and Molecular Biology
College College of Medicine
Campuses Penn State Milton S. Hershey Medical Center
Department Biochemistry and Molecular Biology - HMC
Graduate programs Biochemistry and Molecular Biology
Cell and Molecular Biology
Integrative Biosciences
MD/PhD Degree Program
Email Phone FAX
  jbond@psu.edu
  717 531 8586
  717 531 7072
Educational background
  Ph.D., Rutgers University, 1966
Postdoctoral Training, Vanderbilt University, 1966-1968
Research interests
 

Mechanisms and Regulation of Membane-Bound and Secreted Proteases, Meprins, Metalloendopeptidases

The focus of research in our laboratory is on the structure, function, and regulation of proteolytic enzymes. We are particularly interested in the function, mechanism of action, regulation of biosynthesis, oligomeric assembly and post-translational processing of secreted and cell surface mammalian metalloproteases called meprins.

Our work in mammals and diabetic mice led to the discovery of meprins, plasma membrane and secreted metalloproteases. Meprins can hydrolyze large proteins, polypeptides such as insulin chains and parathyroid hormone, and small biologically active peptides such as bradykinin and gastrin. Meprins are large metalloproteinases (200,000 - 900,000 Da) that are composed of

Graphic
  Graphic
  Membrane-associated and secreted forms of meprin are shown schematically;
Areas of expertise
 
Cysteine EndopeptidasesTranscription, Genetic
Endoplasmic ReticulumSubtilisins
IntestinesProtein Processing, Post-Translational
Chromosome MappingPromoter Regions (Genetics)
Chromosomes, Human, Pair 18Chromosomes, Human, Pair 6
DNA, ComplementaryEndopeptidases
Gene Expression Regulation, DevelopmentalMultienzyme Complexes
Kidney CortexGene Expression
NeoplasmsKidney
Gene Expression Regulation, EnzymologicMetalloendopeptidases
Gene Expression Regulation, NeoplasticAlternative Splicing
Molecular ChaperonesHydronephrosis
OligosaccharidesEducation, Medical
Faculty, MedicalTeaching
Kidney Failure, AcuteMicrovilli
Kidney DiseasesEvolution
Membrane ProteinsPeptide Mapping
Substrate SpecificityCell Membrane
Immunoenzyme TechniquesSalivary Glands
BradykininProtein Precursors
ArginaseDiabetes Mellitus, Experimental
LiverMembrane Glycoproteins
Fructose-Bisphosphate AldolaseAmino Acids, Sulfur
Peptide HydrolasesCells
ProteinsH-2 Antigens
Major Histocompatibility ComplexLinkage (Genetics)
Adenosine TriphosphateCathepsins
EndocytosisInsulin
Mice, Inbred StrainsBlood Proteins
CytosolLysosomes
Antibiotics, AntineoplasticLipopolysaccharides
Cyclic AMPDNA
RNARegeneration
Glyceraldehyde-3-Phosphate DehydrogenasesLactose Intolerance
ZincCell Surface Extensions
Epithelial CellsPeptides
Extracellular SpaceCell Movement
Extracellular MatrixGene Deletion
LeukocytesProtein Subunits
GlobinsReplication Origin
Evolution, MolecularGenes
MiceDisulfides
Protein Structure, QuaternaryGastrointestinal Diseases
Urinary Tract InfectionsAmidines
Antineoplastic AgentsBreast Neoplasms
EflornithineIndans
Matrix Metalloproteinase 7Ornithine Decarboxylase
Publication author name
  Bond JS
Bond J
Select publications
  Norman LP. Jiang W. Han X. Saunders TL. Bond JS. Targeted disruption of the meprin beta gene in mice leads to underrepresentation of knockout mice and changes in renal gene expression profiles. 2003 Feb. Mol Cell Biol. 23(4):1221-30.
National Cancer Institute
National Institute of Diabetes and Digestive and Kidney Diseases
Bertenshaw GP. Norcum MT. Bond JS. Structure of homo- and hetero-oligomeric meprin metalloproteases. Dimers, tetramers, and high molecular mass multimers. 2003 Jan 24. J Biol Chem. 278(4):2522-32.
National Institute of Diabetes and Digestive and Kidney Diseases
Villa JP. Bertenshaw GP. Bond JS. Critical amino acids in the active site of meprin metalloproteinases for substrate and peptide bond specificity. 2003 Oct 24. J Biol Chem. 278(43):42545-50.
National Institute of Diabetes and Digestive and Kidney Diseases
Crisman JM. Zhang B. Norman LP. Bond JS. Deletion of the mouse meprin beta metalloprotease gene diminishes the ability of leukocytes to disseminate through extracellular matrix. 2004 Apr 1. J Immunol. 172(7):4510-9.
National Cancer Institute
National Institute of Diabetes and Digestive and Kidney Diseases
Hengst JA. Bond JS. Transport of meprin subunits through the secretory pathway: role of the transmembrane and cytoplasmic domains and oligomerization. 2004 Aug 13. J Biol Chem. 279(33):34856-64.
National Institute of Diabetes and Digestive and Kidney Diseases

also ...
All publications