Function of the cell adhesion molecule JAM-A in tumour cells:
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| 245 | 1 | 0 | |a Function of the cell adhesion molecule JAM-A in tumour cells |c vorgelegt von Daniel Kummer aus Aachen |
| 264 | 1 | |a Münster |c 2017 | |
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| 502 | |b Dissertation |c Westfälische Wilhelms-Universität Münster |d 2017 |g Beschränkt für den Austausch | ||
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| _version_ | 1804178952903720960 |
|---|---|
| adam_text | TABLE OF CONTENTS
ABSTRACT........................................................................................................................................................1
1.
INTRODUCTION.............................................................................................................................................
3
1.1 THE
EPITHELIUM..................................................................................................................................3
1.1.2 CELL-CELL CONTACTS IN THE
EPITHELIUM...................................................................................3
1.2 PROTEINS OF THE JAM FAM
ILY............................................................................................................
7
1.2.1 JAM
-A.........................................................................................................................................8
1.2.1.1 STRUCTURE OF
JAM-A...............................................................................................................
9
1.2.1.2 FUNCTIONS OF
JAM-A.............................................................................................................
11
1.2.1.2.1 CELL
MIGRATION..............................................................................................................
11
1.2.1.2.2 CELL
POLARITY..................................................................................................................
12
1.2.1.2.3
INFLAMMATION...............................................................................................................
13
1.2.1.2.4
ANGIOGENESIS................................................................................................................
14
1.2.1.2.5
HAEMOSTASIS................................................................................................................
14
1.2.1.2.6 SPINDLE
ORIENTATION......................................................................................................15
1.2.1.2.7 JAM-A AS A VIRUS
RECEPTOR...........................................................................................
16
1.2.2
JAM-8........................................................................................................................................16
1.2.3
JAM-C........................................................................................................................................17
1.2.4 JAM4 AND
JAML.....................................................................................................................
18
1.3
TETRASPANINS...................................................................................................................................
20
1.3.1 STRUCTURE OF
TETRASPANINS....................................................................................................
20
1.3.2 TETRASPANIN - ENRICHED MICRODOMAINS
(TEMS)...............................................................22
1.4 THE
LAMELLIPODIUM.........................................................................................................................23
1.4.1 REGULATION OF LAMELLIPODIAL
ACTIVITY...................................................................................
24
2. AIM OF THIS
THESIS..................................................................................................................................26
3. MATERIALS AND M
ETHODS.......................................................................................................................27
3.1
MATERIALS........................................................................................................................................27
3.1.1 CHEMICALS AND
REAGENTS......................................................................................................
27
3.1.2 KITS AND SPECIAL
REAGENTS.....................................................................................................
30
3.1.3 STANDARD
MARKERS..................................................................................................................31
3.1.4
LABWARE...................................................................................................................................
31
3.1.5
DEVICES....................................................................................................................................
32
3.1.6 SHORT HAIRPIN
RNAS................................................................................................................33
3.1.7 SHORT INTERFERING
RNAS.........................................................................................................34
3.1.8 BACTERIAL STRAINS
3.1.9 PLASMIDS..
3.1.10 CELL
LINES.................................................................................................................................35
3.1.11 STABLE CELL
LINES....................................................................................................................
35
3.1.12
MEDIA.....................................................................................................................................
36
3.1.13 BIOTINYLATED
PEPTIDES.........................................................................................................37
3.1.14 BUFFERS AND
SOLUTIONS..........................................................................................................38
3.1.15 SOFTW
ARE................................................................................................................................39
3.2
ANTIBODIES.......................................................................................................................................
40
3.2.1 PRIMARY
ANTIBODIES................................................................................................................40
3.2.2 SECONDARY
ANTIBODIES...........................................................................................................
41
3.2
METHODS...........................................................................................................................................42
3.2.1 MOLECULAR BIOLOGICAL
METHODS............................................................................................
42
3.2.1.1 CULTIVATION AND CRYOPRESERVATION OF PROKARYOTIC CELLS
...................................................
42
3.2.1.2 TRANSFORMATION OF ELECTROCOMPETENT CELLS
......................................................................
42
3.2.1.3 TRANSFORMATION OF BACTERIA VIA HEAT SHOCK
.......................................................................
42
3.2.1.4 ISOLATION OF PLASMID DNA FROM TRANSFORMED BACTERIA
....................................................
42
3.2.1.5 AGAROSE GEL
ELECTROPHORESIS..............................................................................................
43
3.2.1.6 GEL EXTRACTION OF
DNA.........................................................................................................43
3.2.1.7 QUANTIFICATION OF NUCLEIC
ACIDS..........................................................................................
43
3.2.1.8 DNA
SEQUENCING.................................................................................................................
43
3.2.1.9 RESTRICTION DIGESTION OF
DNA.............................................................................................
44
3.2.1.10
OLIGONUCLEOTIDE-ANNEALING..............................................................................................
44
3.2.1.11 LIGATION OF DNA FRAGMENTS INTO A LINEARIZED PLASMID
...................................................
44
3.2.1.12 PRECIPITATION OF
DNA.........................................................................................................45
3.2.2 PROTEIN BIOCHEMICAL AND IMMUNOBIOCHEMICAL METHODS
.............................................
45
3.2.2.1 QUANTIFICATION OF PROTEINS VIA UV SPECTROPHOTOMETRY
...................................................
45
3.2.2.2 QUANTIFICATION OF PROTEINS VIA BCA PROTEIN
ASSAY............................................................45
3.2.2.3 SDS POLYACRYLAMIDE GEL ELECTROPHORESIS
(SDS-PAGE).......................................................45
3.2.2 4 COOMASSIE STAINING OF PROTEINS IN POLYACRYLAMIDE GELS
..................................................
46
3.2.25
AUTORADIOGRAPHY................................................................................................................
46
3.2.2 6 IN VITRO TRANSCRIPTION AND
TRANSLATION................................................................................46
3.2.2.7 IN VITRO BINDING ANALYSIS VIA GST PULLDOWN
......................................................................
47
3.2.2.8 PEPTIDE PULLDOWNS FROM CELL
LYSATES..................................................................................47
3.2.2 9 IN VITRO KINASE
ASSAY............................................................................................................
48
3.2.2.10 PURIFICATION OF GST FUSION PROTEINS FROM E.COLI LYSATES
.................................................
48
3.2.2.11 WESTERN BLOT
ANALYSIS.......................................................................................................49
3.2.2.12 PREPARATION OF EUKARYOTIC CELL LYSATES
...........................................................................
50
3.2.2.13
CO-IMMUNOPRECIPITATION..................................................................................................50
3.2.2.14 IMMUNOFLUORESCENCE STAINING OF
CELLS.............................................................................51
3.2.2.15 COATING OF CELL CULTURE
PLATES..........................................................................................
52
3.2.3 CELL BIOLOGICAL M
ETHODS........................................................................................................52
3.2.3.1 GROWTH
CONDITIONS..............................................................................................................
52
3.2.3.2 PASSAGING OF EUKARYOTIC CELLS
.............................................................................................
52
3.2.3 3 CRYOPRESERVATION OF EUKARYOTIC
CELLS................................................................................52
3.2.3.3 TRANSIENT TRANSFECTION OF EUKARYOTIC
CELLS.......................................................................
53
3.2.3.4 STABLE TRANSFECTION OF EUKARYOTIC
CELLS..............................................................................53
3.2.3.5 LENTIVIRAL TRANSDUCTION OF EUKARYOTIC
CELLS......................................................................
54
3.2.3.6 STARVATION AND STIMULATION OF EUKARYOTIC
CELLS................................................................54
3.2.3.7 SRC FAMILY KINASE (SFK) INHIBITION OF MCF-7
CELLS.............................................................55
3.2.4 FUNCTIONAL
ASSAYS...................................................................................................................
55
3.2.4.1 INVASION OF EUKARYOTIC
CELLS................................................................................................55
3.2.4.2 MOTILITY OF MCF-7
CELLS.......................................................................................................55
3.2.5 STATISTICAL
ANALYSIS..................................................................................................................55
4.
RESULTS..................................................................................................................................................56
4.1 CHARACTERISATION OF A TETRAMERIC PROTEIN COMPLEX IN MCF-7 CELLS
....................................
56
4.1.1 JAM-A INTERACTS WITH TETRASPANIN CD9 IN MCF-7 CELLS
...................................................
56
4.1.2 CD81 IS A NEW INTERACTION PARTNER OF JAM-A IN MCF-7
CELLS........................................57
4.1.3 CD9 AND CD81 INTERACT IN MCF-7
CELLS...............................................................................58
4.1.4 JAM-A INTERACTS WITH INTEGRIN
OIVSSS...................................................................................
59
4.1.5 CD9 INTERACTS WITH INTEGRIN
OIVSSS........................................................................................61
4.1.6 CD81 INTERACTS WITH INTEGRIN
OIVSSS.....................................................................................
61
4.1.7 CD9 AND CD81 TOGETHER MEDIATE THE INTERACTION OF JAM-A AND
INTEGRIN OIVSSS
.......
63
4.2 CHARACTERISATION OF THE INTERACTION BETWEEN JAM-A AND CD81
.........................................
65
4.3 THE TETRAMERIC COMPLEX LOCALISES TO LAMELLIPODIA IN MCF-7
CELLS......................................68
4.3.1 INTEGRIN OIVSSS LOCALISES TO
LAMELLIPODIA..............................................................................68
4.3.2 JAM-A LOCALISES TO LAMELLIPODIA AND COLOCALISES WITH INTEGRIN
OIVSSS
...........................
69
4.3.3 JAM-A PARTIALLY COLOCALISES WITH CD81 AT THE PERIPHERY OF THE
CELLS
.........................
70
4.3.4 CD9 COLOCALISES WITH JAM-A AT
LAMELLIPODIA..................................................................
72
4.4 DOWNSTREAM EFFECTORS OF THE TETRAMERIC COMPLEX IN MCF-7
CELLS.....................................73
4.4.1 JAM-A INTERACTS WITH TYROSINE KINASE C-SRC
....................................................................
73
4.4.2 TYROSINE KINASE C-SRC IS ASSOCIATED WITH THE TETRAMERIC
COMPLEX..............................77
4.4.3 JAM-A REGULATES C-SRC ACTIVITY IN A NEGATIVE REGULATORY M
ANNER...............................78
4.4.4 THE TERNARY COMPLEX REGULATES ERK-PHOSPHORYLATION IN A NEGATIVE
REGULATORY
M
ANNER.............................................................................................................................................
81
4.4.5 JAM-A REGULATES THE WAVE REGULATORY COMPLEX COMPONENT A B IL
...........................
85
4.5 JAM-A TYROSINE PHOSPHORYLATION THROUGH SFKS IN MCF-7 CELLS
..........................................
86
4.5.1 JAM-A IS PHOSPHORYLATED BY C-SRC AT TYROSINE 280 IN V ITRO
.........................................
86
4.5.2 C-SRC PHOSPHORYLATES JAM-A AT TYROSINE 280 IN HEK293T CELLS
..................................
87
4.5.3 TYROSINE 280-PHOSPHORYLATED JAM-A IS DETECTED SPECIFICALLY BY THE
AFFIL550-N
ANTIBODY.............................................................................................................................................
88
4.5.4 JAM-A IS TYROSINE 280-PHOSPHORYLATED UPON VEGF
STIMULATION................................90
4.5.5 TYROSINE PHOSPHORYLATION OF ENDOGENOUS JAM-A IS MEDIATED BY SRC
FAMILY KINASES
92
4.5.6 TYROSINE 280-PHOSPHORYLATED JAM-A LOCALISES TO LAMELLIPODIA IN
RESPONSE TO VEGF
93
4.6 INTERACTION PARTNERS OF TYROSINE 280-PHOSPHORYLATED
JAM-A..............................................95
4.6.1 C-SRC REGULATOR CSK AND TYROSINE PHOSPHATASE SHP-2 BIND TO
PY280-JAM-A
.........
95
4.6.2 CSK IS ASSOCIATED WITH THE TETRAMERIC COMPLEX IN MCF-7 CELLS
..................................
98
4.7 FUNCTIONAL ANALYSES OF THE TETRAMERIC COMPLEX
...................................................................
100
4.7.1 DISRUPTION OF THE TETRAMERIC COMPLEX PROMOTES DETACHMENT OF CELLS
FROM THE
COLLECTIVE..........................................................................................................................................
100
4.7.2 DEPLETION OF CD9 AND CD81 ENHANCES MCF-7 SINGLE CELL M IGRATION
.......................
102
5.
DISCUSSION..........................................................................................................................................
104
5.1 JAM-A, CD9, CD81 AND INTEGRIN CXVSSS FORM A TETRAMERIC COMPLEX IN
MCF-7 CELLS
........
104
5.2 CD81 IS A NEW BINDING PARTNER OF
JAM-A...............................................................................105
5.3 DOWNSTREAM EFFECTORS OF THE TETRAMERIC COMPLEX IN MCF-7 CELLS
..................................
107
5.3.1 C-SRC IS ASSOCIATED WITH THE TETRAMERIC COM PLEX
.........................................................
107
5.3.2 C-SRC ACTIVITY IS NEGATIVELY REGULATED BY
JAM-A.............................................................107
5.3.2.1 JAM-A IS PHOSPHORYLATED BY C-SRC AT TYROSINE 280 AND THE
AFFIL550-N ANTIBODY
SPECIFICALLY DETECTS
PY280-JAM-A.................................................................................................108
5.3.2.2 JAM-A IS PHOSPHORYLATED AT TYROSINE 280 UPON VEGF STIMULATION
.............................
109
5.3.3 C-TERMINAL SRC KINASE INTERACTS WITH TYROSINE280-PHOSPHORYLATED
JAM-A
.............
110
5.3.4 TYROSINE PHOSPHATASE SHP-2 INTERACTS WITH PY280-JAM-A
........................................
110
5.4 JAM-A NEGATIVELY REGULATES ERK1/2-MAPK SIGNALLING IN RESPONSE TO
VEGF
..................
112
5.5 THE TETRAMERIC COMPLEX LOCALISES TO LAMELLIPODIA OF MCF-7 CELLS
...................................
113
5.6 JAM-A NEGATIVELY REGULATES THE ACTIVITY OF THE WRC SUBUNIT A B IL
.................................
114
5.7 TYROSINE 280-PHOSPHORYLATED JAM-A LOCALISES TO LAMELLIPODIA IN
RESPONSE TO VEGF.. 116
5.8 DISRUPTION OF THE TETRAMERIC COMPLEX ENHANCES COLLECTIVE CELL M
IGRATION
...................
117
5.9 WORKING MODEL OF SIGNALLING MEDIATED BY THE TETRAMERIC COMPLEX
..................................
119
6. SUMMARY AND
OUTLOOK......................................................................................................................
122
7.
APPENDIX...............................................................................................................................................123
7.1 ANALYSES OF A JAM-A - CD9 - CD81 - INTEGRIN AVSSS COMPLEX IN
MDA-MB-231 CELLS.... 123
7.2 FUNCTIONAL ROLE OF JAM-A Y280 PHOSPHORYLATION IN MDA-MB-231
CELLS............................124
7.2.1 GENERATION OF A STABLE MDA-MB-231 CELL LINE WITH INDUCIBLE JAM-A
KNOCKDOWN 124
7.2.2 JAM-A TYROSINE PHOSPHORYLATION REGULATES INVASION OF MDA-MB-231
CELLS
.........
126
7.3 CONCLUDING
REMARKS....................................................................................................................
127
DANKSAGUNG.............................................................................................................................................
130
REFERENCES................................................................................................................................................131
LIST OF
FIGURES...........................................................................................................................................
148
LIST OF
TABLES............................................................................................................................................
149
LIST OF
ABBREVIATIONS...............................................................................................................................149
|
| any_adam_object | 1 |
| author | Kummer, Daniel 1986- |
| author_GND | (DE-588)1150895977 |
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| discipline | Biologie Medizin |
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| language | English |
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| physical | viii, 152 Blätter Illustrationen 30 cm |
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| spelling | Kummer, Daniel 1986- Verfasser (DE-588)1150895977 aut Function of the cell adhesion molecule JAM-A in tumour cells vorgelegt von Daniel Kummer aus Aachen Münster 2017 viii, 152 Blätter Illustrationen 30 cm txt rdacontent n rdamedia nc rdacarrier Dissertation Westfälische Wilhelms-Universität Münster 2017 Beschränkt für den Austausch (DE-588)4113937-9 Hochschulschrift gnd-content B:DE-101 application/pdf http://d-nb.info/1150340797/04 Inhaltsverzeichnis DNB Datenaustausch application/pdf http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=030616564&sequence=000001&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA Inhaltsverzeichnis |
| spellingShingle | Kummer, Daniel 1986- Function of the cell adhesion molecule JAM-A in tumour cells |
| subject_GND | (DE-588)4113937-9 |
| title | Function of the cell adhesion molecule JAM-A in tumour cells |
| title_auth | Function of the cell adhesion molecule JAM-A in tumour cells |
| title_exact_search | Function of the cell adhesion molecule JAM-A in tumour cells |
| title_full | Function of the cell adhesion molecule JAM-A in tumour cells vorgelegt von Daniel Kummer aus Aachen |
| title_fullStr | Function of the cell adhesion molecule JAM-A in tumour cells vorgelegt von Daniel Kummer aus Aachen |
| title_full_unstemmed | Function of the cell adhesion molecule JAM-A in tumour cells vorgelegt von Daniel Kummer aus Aachen |
| title_short | Function of the cell adhesion molecule JAM-A in tumour cells |
| title_sort | function of the cell adhesion molecule jam a in tumour cells |
| topic_facet | Hochschulschrift |
| url | http://d-nb.info/1150340797/04 http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=030616564&sequence=000001&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA |
| work_keys_str_mv | AT kummerdaniel functionofthecelladhesionmoleculejamaintumourcells |
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