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Related Experiment Video

Updated: Feb 18, 2026

Implementing Patch Clamp and Live Fluorescence Microscopy to Monitor Functional Properties of Freshly Isolated PKD Epithelium

Implementing Patch Clamp and Live Fluorescence Microscopy to Monitor Functional Properties of Freshly Isolated PKD Epithelium

Published on: September 1, 2015

A structure-function analysis in patients with prekallikrein deficiency.

Antonio Girolami¹, Silvia Ferrari¹, Elisabetta Cosi¹

¹a Department of Medicine , University of Padua Medical School , Padua , Italy.

Hematology (Amsterdam, Netherlands)

|November 23, 2017

Summary

Prekallikrein (PK) deficiency mutations primarily affect the catalytic domain, with most patients showing no bleeding symptoms. Further molecular studies are crucial for understanding blood coagulation.

Keywords:

Prekallikrein bleeding deficiency hypertension molecular studies

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Last Updated: Feb 18, 2026

Implementing Patch Clamp and Live Fluorescence Microscopy to Monitor Functional Properties of Freshly Isolated PKD Epithelium

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Spectral Karyotyping to Study Chromosome Abnormalities in Humans and Mice with Polycystic Kidney Disease

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Published on: February 3, 2012

Area of Science:

Biochemistry
Hematology
Molecular Biology

Background:

Prekallikrein (PK) is a key protein in the contact phase of blood coagulation.
Recent research has renewed interest in the role of PK.

Purpose of the Study:

To explore the relationship between the structure and function of prekallikrein in individuals with PK deficiency.
To identify and characterize mutations associated with PK deficiency.

Main Methods:

Analysis of patients diagnosed with PK deficiency using molecular biology techniques.
Data collection through personal files and a comprehensive PubMed literature search.
Inclusion criteria focused on molecular-biology-confirmed diagnoses.

Main Results:

Twelve families were included in the study.
Ten missense mutations, three stop codons, and two insertions were identified, predominantly in exons 11 and 14.
Most mutations were located in the catalytic domain, and the majority of patients (11/12) exhibited no bleeding manifestations.

Conclusions:

The majority of identified mutations in prekallikrein deficiency impact the catalytic domain.
Molecular studies are essential for advancing the understanding of the contact phase of blood coagulation.
Future case reports should incorporate molecular findings to enhance comprehension of PK deficiency.