Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Search research articles

Related Experiment Videos

Porcine amelogenins

Y Yamakoshi¹, T Tanabe, M Fukae

¹Department of Biochemistry, School of Dental Medicine, Tsurumi University, Yokohama, Japan.

Calcified Tissue International

|January 1, 1994

Summary

This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

DPP and DSP are Necessary for Maintaining TGF-β1 Activity in Dentin.

Journal of dental research·2014

Same author

Cytodifferentiation activity of synthetic human enamel sheath protein peptides.

Journal of periodontal research·2010

Same author

Effects of porcine 25 kDa amelogenin and its proteolytic derivatives on bone sialoprotein expression.

Journal of periodontal research·2010

Same author

Cleavage site specificity of MMP-20 for secretory-stage ameloblastin.

Journal of dental research·2010

Same author

Degradation of noncollagenous components by neutrophil elastase reduces the mechanical strength of rat periodontal ligament.

Journal of periodontal research·2008

Same author

Splicing determines the glycosylation state of ameloblastin.

Journal of dental research·2007

Same journal

Capsanthin Attenuates Osteoporosis by Targeting the Urotensin II Receptor Pathway to Inhibit Oxidative Stress and NLRP3 Inflammasome Activation.

Calcified tissue international·2026

Same journal

ODAPH (p.Arg77) Phenotype and Onset of Ameloblast Pathology During Postsecretory Transition Demonstrated by FIB-SEM Analyses of Odaph<sup>C41/C41*</sup> Mice.

Calcified tissue international·2026

Same journal

Cytokine Networks Reprogramming the Osteo-Immune Microenvironment in Cancer Bone Metastasis.

Calcified tissue international·2026

Same journal

Associations between controlling nutritional status and mortality in osteoporosis: evidence from NHANES, 2005-2018.

Calcified tissue international·2026

Same journal

Gut Microbiota-Derived TMAO Drives MC3T3-E1 Senescence and Osteogenic Dysfunction via cGAS-STING-NF-κB Signaling: Implications for Age-Related Bone Loss.

Calcified tissue international·2026

Same journal

Artificial Intelligence Approaches for Osteoporotic Fracture Risk Prediction Using Administrative Health Data: A Systematic Review.

Calcified tissue international·2026

See all related articles

Researchers purified porcine amelogenins, identifying at least four types from alternative splicing. Mass spectrometry confirmed the 25 kDa amelogenin lacks phosphorylation and glycosylation, advancing enamel protein research.

Area of Science:

Biochemistry
Molecular Biology
Dental Research

Background:

Amelogenins are the major proteins in developing tooth enamel.
Understanding amelogenin structure and function is crucial for enamel formation research.

Purpose of the Study:

To extract and purify porcine amelogenins.
To characterize the identified amelogenin variants.
To investigate post-translational modifications of porcine 25 kDa amelogenin.

Main Methods:

Extraction of amelogenins from porcine secretory enamel.
Purification using gel filtration and reverse-phase HPLC.
Amino acid sequencing and mass spectrometry analysis.

Main Results:

Related Experiment Videos

Isolation and purification of porcine amelogenins.
Identification of at least four prototype amelogenins resulting from alternative splicing.
Mass spectrometry revealed that porcine 25 kDa amelogenin is not phosphorylated or glycosylated.

Conclusions:

Porcine enamel contains multiple amelogenin variants due to alternative splicing.
The 25 kDa amelogenin isoform lacks common post-translational modifications.
These findings contribute to the understanding of enamel matrix protein heterogeneity and biosynthesis.